Publications by authors named "Mohammad Ali Faramarzi"

144 Publications

Polyherbal combination for wound healing: Matricaria chamomilla L. and Punica granatum L.

Daru 2021 May 9. Epub 2021 May 9.

Department of Pharmaceutics, Faculty of Pharmacy, Tehran University of Medical Sciences, Tehran, Iran.

Background: Punica granatum L. (pomegranate) with astringent activities and Matricaria chamomilla L. (chamomile) with anti-inflammatory and antioxidant properties are natural remedies used for various skin disorders, including wound healing.

Objectives: This study was conducted to evaluate the individual and combined wound healing activity of the methanol extracts of pomegranate and chamomile flowers.

Methods: After preparing the menthol fraction of pomegranate and chamomile flowers, the content of total phenols, total tannins, and total flavonoids of fractions was measured. For standardization of pomegranate and chamomile fractions, Gallic acid and apigenin-7-O-glucoside contents of them were determined using high-performance liquid chromatography (HPLC). Moreover, their antioxidant activities were examined using DPPH and FRAP tests. The antimicrobial assay was performed against Staphylococcus aureus, Staphylococcus epidermidis, and Pseudomonas aeruginosa. Three different concentrations of methanol fraction of each plant and one combination dose of fractions were investigated for their wound healing activities in an excision wound model on the rats' dorsum. Finally, histopathological studies were done at the end of the experiment.

Results: Phytochemical examinations showed high amounts of phenolic compounds in pomegranate flowers, while chamomile flower fractions contained a high amount of total flavonoids. Both fractions, especially pomegranate, had potent antioxidant activity. The best results for wound closure were observed 7 days after wound induction. All treated groups exhibited superior wound contraction compared to their placebo at all measurement times. The combined form of pomegranate and chamomile had better wound healing properties compared to a single therapy, especially on time earlier to wound induction.

Conclusion: This study represented high antioxidant and wound healing activities for methanol fraction of pomegranate and chamomile flowers, which could be related to their high content of phytochemicals. In comparison with single herb treatment, the combined form of these two fractions in lower concentrations accelerated wound closure.
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http://dx.doi.org/10.1007/s40199-021-00392-xDOI Listing
May 2021

Synthesis, in vitro evaluation, and molecular docking studies of novel hydrazineylideneindolinone linked to phenoxymethyl-1,2,3-triazole derivatives as potential α-glucosidase inhibitors.

Bioorg Chem 2021 Mar 29;111:104869. Epub 2021 Mar 29.

Medicinal Plants Research Center, Faculty of Pharmacy, Tehran University of Medical Sciences, Tehran, Iran; Persian Medicine and Pharmacy Research Center, Tehran University of Medical Sciences, Tehran, Iran. Electronic address:

In this work, a novel series of hydrazineylideneindolinone linked to phenoxymethyl-1,2,3-triazole derivatives were designed, synthesized, and evaluated for their anti-α-glucosidase activity due to an urgent need to develop effective anti-diabetic agents. Among tested 15 compounds, 8 derivatives (9a, 9b, 9c, 9d, 9e, 9f, 9h, and 9o) demonstrated superior potency compared to that of positive control, acarbose. Particularly, compound 9d possessed the best anti-α-glucosidase activity with around a 46-fold improvement in the inhibitory activity. Additionally, 9d showed a competitive type of inhibition in the kinetic study and the molecular docking study demonstrated that it well occupied the binding pocket of the catalytic center through desired interactions with residues, correlating to the experimental results.
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http://dx.doi.org/10.1016/j.bioorg.2021.104869DOI Listing
March 2021

1, 5-dicaffeoylquinic acid, an α-glucosidase inhibitor from the root of D. Don.

Res Pharm Sci 2020 Oct 19;15(5):429-436. Epub 2020 Oct 19.

Department of Pharmacognosy, Faculty of Pharmacy, Tehran University of Medical Sciences, Tehran, I.R. Iran.

Background And Purpose: D. Don (Apiaceae family) is a perennial plant whose oleo- gum resin is used as a natural remedy for various diseases, especially chronic bronchitis, and asthma. In the present study, hydromethanolic extract of root was subjected to phytochemical analyses and α-glucosidase inhibitory potentials of the isolated compounds were assessed.

Experimental Approach: Silica gel (normal and reversed phases) and Sephadex LH-20 column chromatographies were used for the isolation and purification of the compounds. Structures of the compounds were characterized by 1D and 2D nuclear magnetic resonance (NMR) techniques. All the isolated compounds were assessed for their α-glucosidase inhibitory activity in comparison with acarbose, a standard drug.

Findings/results: Two phloroacetophenone glycosides; echisoside () and pleoside (), along with dihydroferulic acid-4-O-β-D-glucopyranoside (), and β-resorcylic acid (), and two caffeoylquinic acid derivatives; chlorogenic acid () and 1, 5-dicaffeoylquinic acid (cynarin, ) were isolated. Among the isolated compounds, the α-glucosidase inhibitory effect of 1,5-dicaffeoylquinic acid was found as 76.9% of the acarbose activity at 750 μM (IC value of acarbose).

Conclusion And Implications: Considerable α-glucosidase inhibitory effect of 1,5-dicaffeoylquinic acid makes it an appropriate candidate for further studies in the development of new natural antidiabetic drugs.
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http://dx.doi.org/10.4103/1735-5362.297845DOI Listing
http://www.ncbi.nlm.nih.gov/pmc/articles/PMC7879791PMC
October 2020

Quinazolinone-dihydropyrano[3,2-b]pyran hybrids as new α-glucosidase inhibitors: Design, synthesis, enzymatic inhibition, docking study and prediction of pharmacokinetic.

Bioorg Chem 2021 Apr 8;109:104703. Epub 2021 Feb 8.

Nano Alvand Company, Avicenna Tech Park, Tehran University of Medical Sciences, Tehran, Iran. Electronic address:

A series of new quinazolinone-dihydropyrano[3,2-b]pyran derivatives 10A-L were synthesized by simple chemical reactions and were investigated for inhibitory activities against α-glucosidase and α-amylase. New synthesized compounds showed high α-glucosidase inhibition effects in comparison to the standard drug acarbose and were inactive against α-amylase. Among them, the most potent compound was compound 10L (IC value = 40.1 ± 0.6 µM) with inhibitory activity around 18.75-fold more than acarboase (IC value = 750.0 ± 12.5 µM). This compound was a competitive inhibitor into α-glucosidase. Our obtained experimental results were confirmed by docking studies. Furthermore, the cytotoxicity of the most potent compounds 10L, 10G, and 10N against normal fibroblast cells and in silico druglikeness, ADME, and toxicity prediction of these compounds were also evaluated.
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http://dx.doi.org/10.1016/j.bioorg.2021.104703DOI Listing
April 2021

Synthesis, in-vitro evaluation, molecular docking, and kinetic studies of pyridazine-triazole hybrid system as novel α-glucosidase inhibitors.

Bioorg Chem 2021 Apr 1;109:104670. Epub 2021 Feb 1.

Drug Design and Development Research Center, The Institute of Pharmaceutical Sciences (TIPS), Tehran University of Medical Sciences, Tehran, Iran; Department of Medicinal Chemistry, Faculty of Pharmacy, Tehran University of Medical Sciences, Tehran, Iran. Electronic address:

In this study, we reported the discovery of pyridazine based 1,2,3-triazole derivatives as inhibitors of α-glucosidase. All target compounds exhibited significant inhibitory activities against yeast and rat α-glucosidase enzymes compared to positive control, acarbose. The most potent compound 6j, ethyl 3-(2-(1-(4-nitrobenzyl)-1H-1,2,3-triazol-4-yl)ethyl)-5,6-diphenylpyridazine-4-carboxylate exhibited IC values of 58, and 73 µM. Docking studies indicated the responsibility of hydrophobic and hydrogen bonding interactions in the ligand-enzyme complex stability. The in-vitro safety against the normal cell line was observed by toxicity evaluation of the selected compounds.
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http://dx.doi.org/10.1016/j.bioorg.2021.104670DOI Listing
April 2021

Phytocatalytic and cytotoxic activity of the purified laccase from bled resin of Pistacia atlantica Desf.

Int J Biol Macromol 2021 Apr 3;176:394-403. Epub 2021 Feb 3.

Department of Pharmaceutical Biotechnology, Faculty of Pharmacy, Tehran University of Medical Sciences, P.O. Box 14155-6451, Tehran 1417614411, Iran. Electronic address:

This study reports an efficient and fast procedure for the purification of laccase (PaL) obtained from the resin of Pistacia atlantica Desf. It was purified by one-step affinity chromatography and showed the specific activity of 393 U/mg with 81.9-fold purification. The molecular weight of PaL was estimated to be approximately 60 kDa using gel electrophoresis SDS-PAGE. Moreover, it depicted diphenolase activity and high affinity towards 2,6-dimethoxy phenol (K = 10.01 ± 0.5 mM) and syringaldazine (K = 6.57 ± 0.2 mM) comparing with plant-origin polyphenol oxidases reported in the literature. It should be noted that PaL possessed optimal activity at pH 7.5 and 45 °C. It also remained stable under different conditions of pH (6.5-8.0), temperature (25-45 °C), and when it was exposed to several metal ions. The MTT and flow cytometry assays demonstrated that the enzyme treatment significantly affected growth of HeLa, HepG2, and MDA-MB-231 cells with LC values of 4.83 ± 0.02, 61 ± 0.31, and 26.83 ± 0.11 μM after 72 h, respectively. NOVELTY STATEMENT: This is the first attempt to isolate and characterize a new oxidoreductase from the resin of Pistacia atlantica Desf., native species of Iran, to recruit it in cytotoxicity researches. In the purification process by an efficient affinity column (SBA-NH-GA), the enzyme was eluted promptly with a satisfied yield. The purified laccase exerted higher affinity to diphenolic compounds and pH-thermal stability compared to other plant-derived polyphenol oxidases. The purified enzyme was found to show anti-oxidant capacity and significantly inhibited the growth of cancerous cells in vitro. PaL showed more cytotoxic activity towards HeLa and MDA-MB-231 cells by induction of apoptosis. The cytotoxic activity of the laccase was measured by flow cytometry.
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http://dx.doi.org/10.1016/j.ijbiomac.2021.01.212DOI Listing
April 2021

Development of an enzyme-enhancer system to improve laccase biological activities.

Int J Biol Macromol 2021 Mar 15;173:99-108. Epub 2021 Jan 15.

Department of Drug and Food Control, Faculty of Pharmacy, Tehran University of Medical Sciences, P.O. Box 14155-6451, Tehran 1417614411, Iran; Pharmaceutical Quality Assurance Research Center, The Institute of Pharmaceutical Sciences (TIPS), Tehran University of Medical Sciences, Tehran, Iran. Electronic address:

The present investigation reports an in-vitro study using combination of laccase and an enhancer capable of inhibiting the growth of pathogenic microorganisms, preventing biofilm formation, and whitening teeth. Laccase-cinnamic acid system remarkably inhibited the growth of Aggregatibacter actinomycetemcomitans, Candida albicans, S. aureus, and Streptococcus mutans whilst showed no significant effects on Gram-negative bacteria. Data presented that cinnamic acid (10 mM) with laccase (0.125 U ml) led to a maximum decrease of about 90%, in S. mutans biofilm formation. The confocal laser scanning microscopy showed considerable detachment of S. mutans cells from glass substratum. The combined laccase-cinnamic acid system could remove teeth discoloration caused by coffee. SEM of the teeth surface exhibited no damages such as surface cracking or fracture. Liquid chromatography-tandem mass spectrometry (LC-MS) and cyclic voltammetry (CV) studies showed that laccase can catalyze the one-electron oxidation of cinnamic acid to the respective radical. This radical can then undergo several fates, including recombination with another radical to form a dimeric species, dismutation of the radical back to cinnamic acid or decarboxylation to give various reduced oxygen species. Therefore, the redox potential values of phenolic monomers/oligomers are related with their biological activities.
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http://dx.doi.org/10.1016/j.ijbiomac.2021.01.068DOI Listing
March 2021

Lipase@zeolitic imidazolate framework ZIF-90: A highly stable and recyclable biocatalyst for the synthesis of fruity banana flavour.

Int J Biol Macromol 2021 Jan 6;166:1301-1311. Epub 2020 Nov 6.

Department of Pharmaceutical Biotechnology, Faculty of Pharmacy, Tehran University of Medical Sciences, P.O. Box 14155-6451, Tehran 1417614411, Iran. Electronic address:

A zeolitic imidazolate framework (ZIF-90) has been synthesized through solvothermal method. The structure was characterized by means of FT-IR spectroscopy, X-ray diffraction, thermogravimetric analysis (TGA), and scanning electron microscopy (SEM)/energy dispersive X-ray spectroscopy (EDS). The synthesized ZIF-90 was applied as a support for immobilization of porcine pancreatic lipase (PPL). The immobilized enzyme (PPL@ZIF-90) exhibited immobilization yield and efficiency of 66 ± 1.8% and 89 ± 1.4%, respectively. The pH and thermal stability of PPL was improved after immobilization and the initial activity was retained at about 57% after 20 days of storage at 4 °C for PPL@ZIF-90. Moreover, about 57% of the original activity was remained following 10 cycles of application. In Michaelis-Menten kinetic studies, K value for PPL@ZIF-90 was lower, while, the V was higher than free PPL. Moreover, optimized conditions to produce fruity banana flavour upon esterification of butyric acid were investigated. The optimum esterification yield was 73.79 ± 1.31% in the presence of 245 mg PPL@ZIF-90, alcohol/acid ratio of 2.78 and 39 h reaction time. PPL@ZIF-90 showed 39% relative esterification yield after six cycles of reuse. The results suggested that PPL@ZIF-90 can be used as a potential effective biocatalyst for synthesis of isoamyl butyrate.
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http://dx.doi.org/10.1016/j.ijbiomac.2020.11.011DOI Listing
January 2021

Design and synthesis of novel pyrazole-phenyl semicarbazone derivatives as potential α-glucosidase inhibitor: Kinetics and molecular dynamics simulation study.

Int J Biol Macromol 2021 Jan 4;166:1082-1095. Epub 2020 Nov 4.

Endocrinology and Metabolism Research Center, Endocrinology and Metabolism Research Institute, Tehran University of Medical Sciences, Tehran, Iran. Electronic address:

A series of novel pyrazole-phenyl semicarbazone derivatives were designed, synthesized, and screened for in vitro α-glucosidase inhibitory activity. Given the importance of hydrogen bonding in promoting the α-glucosidase inhibitory activity, pharmacophore modification was established. The docking results rationalized the idea of the design. All newly synthesized compounds exhibited excellent in vitro yeast α-glucosidase inhibition (IC values in the range of 65.1-695.0 μM) even much more potent than standard drug acarbose (IC = 750.0 μM). Among them, compounds 8o displayed the most potent α-glucosidase inhibitory activity (IC = 65.1 ± 0.3 μM). Kinetic study of compound 8o revealed that it inhibited α-glucosidase in a competitive mode (Ki = 87.0 μM). Limited SAR suggested that electronic properties of substitutions have little effect on inhibitory potential of compounds. Cytotoxic studies demonstrated that the active compounds (8o, 8k, 8p, 8l, 8i, and 8a) compounds are also non-cytotoxic. The binding modes of the most potent compounds 8o, 8k, 8p, 8l and 8i was studied through in silico docking studies. Molecular dynamic simulations have been performed in order to explain the dynamic behavior and structural changes of the systems by the calculation of the root mean square deviation (RMSD) and root mean square fluctuation (RMSF).
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http://dx.doi.org/10.1016/j.ijbiomac.2020.10.263DOI Listing
January 2021

Immobilization of lipase on the modified magnetic diatomite earth for effective methyl esterification of isoamyl alcohol to synthesize banana flavor.

3 Biotech 2020 Oct 23;10(10):447. Epub 2020 Sep 23.

Department of Pharmaceutical Biotechnology, Faculty of Pharmacy, Tehran University of Medical Sciences, P.O. Box 14155-6451, 1417614411 Tehran, Iran.

The present study was designed to propose a simple, cost-effective, and efficient method for the preparation of a biocompatible composite made from magnetic diatomaceous earth (mDE) coated by aminopropyltriethoxysilane (APTES) and its application for immobilization of porcine pancreatic lipase (PPL). The produced mDE-APTES was instrumentally characterized and the obtained results of FTIR analysis and scanning electron microscopy equipped by energy-dispersive X-ray spectroscopy (SEM-EDS) showed successful coating of APTES on mDE surface. PPL was then immobilized onto mDE to obtain the biocatalyst of PPL@mDE (immobilization yield and efficiency of 78.0 ± 0.3% and 80.1 ± 0.6, respectively) and the presence of enzyme was confirmed by EDS method. The attained results of the reusability of PPL@mDE revealed that 57% of the initial activity was retained after 11 cycles of biocatalyst application. PPL@mDE demonstrated higher storage stability than the free enzyme at 4 °C, 25 °C, and 37 °C. The apparent (2.35 ± 0.12 mM) and (13.01 ± 0.64 µmol/min) values for the immobilized enzyme were considerably altered compared to those of the free enzyme ( > 0.05). PPL@mDE was subsequently employed for the synthesis of banana flavor (isoamyl acetate) in -hexane, which yields an esterification percentage of 100 at 37 °C after 3 h. However, it merits further investigations to find out about large-scale application of the as-synthesized biocatalyst for esterification.
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http://dx.doi.org/10.1007/s13205-020-02437-5DOI Listing
http://www.ncbi.nlm.nih.gov/pmc/articles/PMC7511503PMC
October 2020

Synthesis of 4-alkylaminoimidazo[1,2-a]pyridines linked to carbamate moiety as potent α-glucosidase inhibitors.

Mol Divers 2020 Oct 12. Epub 2020 Oct 12.

Persian Medicine and Pharmacy Research Center, Tehran University of Medical Sciences, Tehran, Iran.

In this work, various imidazo[1,2-a]pyridines linked to carbamate moiety were designed, synthesized, and evaluated for their α-glucosidase inhibitory activity. Among synthesized compounds, 4-(3-(tert-Butylamino)imidazo[1,2-a]pyridin-2-yl)phenyl p-tolylcarbamate (6d) was the most potent compound (IC = 75.6 µM) compared with acarbose as the reference drug (IC = 750.0 µM). Kinetic study of compound 6d indicated a competitive inhibition. Also, the molecular docking study suggested desired interactions with the active site residues. In particular, hydrogen bonds and electrostatic interactions constructed by compound 6d afforded well-oriented conformation in the 3A4A active site.
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http://dx.doi.org/10.1007/s11030-020-10137-8DOI Listing
October 2020

Application of Electrospray in Preparing Solid Lipid Nanoparticles and Optimization of Nanoparticles Using Artificial Neural Networks.

Avicenna J Med Biotechnol 2020 Oct-Dec;12(4):251-254

Natural Products and Medicinal Plants Research Center, North Khorasan University of Medical Sciences, Bojnurd, Iran.

Background: Electrospray (Electrohydrodynamic atomization) has been introduced as a novel approach to prepare nanoparticles. This work aimed to prepare SLNs through electrospray and evaluate factors affecting particle size of prepared Solid Lipid Nanoparticles (SLNs).

Methods: SLNs were prepared by electrospray method. To study the factors affecting particle size of SLNs, Artificial Neural Networks (ANNs) were employed. Four input variables, namely, Tween 80 concentration, lipid concentration, flow rate, and polymer to lipid ratio were analyzed through ANNs and particle size was the output.

Results: The analyzed model presented concentration of Tween 80 (surfactant) and lipid as effective parameters on particle size. By increasing surfactant and decreasing lipid concentration, minimum size could be obtained, while flow rate and polymer to lipid ratio appeared not to be effective.

Conclusion: Concentration of surfactant/lipid plays the most important role in determining the size.
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http://www.ncbi.nlm.nih.gov/pmc/articles/PMC7502161PMC
October 2020

An organic solvent-tolerant lipase of MV1 with the potential application for enzymatic improvement of n6/n3 ratio in polyunsaturated fatty acids from fenugreek seed oil.

J Food Sci Technol 2020 Sep 17:1-12. Epub 2020 Sep 17.

Department of Pharmaceutical Biotechnology, Faculty of Pharmacy, Tehran University of Medical Sciences, P.O. Box 14155-6451, 1417614411 Tehran, Iran.

Lipase-catalyzed esterification is an efficient technique in the production of polyunsaturated fatty acid (PUFA) concentrates which are applied for nutrition and health purposes. In this project, a solvent-tolerant lipase from MV1 was immobilized and purified by a hydrophobic support. The purified lipase revealed enhanced activity and stability towards chemicals, organic solvents, and a broad range of pH values. The production of lipase was enhanced to 7.0 U/mL after optimization by a central composite design. Acylglycerols (AGs) rich in α-linolenic acid (45%, w/w) were produced and a favorable n-6/n-3 free fatty acid (FFA) ratio of 1.1 was achieved in fenugreek seed oil using the immobilized lipase. The ability of lipase in ester synthesis and the improvement of n6/n3 FFA ratio make it a suitable candidate in food production industries.
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http://dx.doi.org/10.1007/s13197-020-04784-wDOI Listing
http://www.ncbi.nlm.nih.gov/pmc/articles/PMC7498116PMC
September 2020

Optimization of immobilization conditions of Bacillus atrophaeus FSHM2 lipase on maleic copolymer coated amine-modified graphene oxide nanosheets and its application for valeric acid esterification.

Int J Biol Macromol 2020 Nov 16;162:1790-1806. Epub 2020 Aug 16.

Pharmaceutical Sciences and Cosmetic Products Research Center, Kerman University of Medical Sciences, Kerman, Iran; Department of Pharmaceutical Biotechnology, Faculty of Pharmacy, Kerman University of Medical Sciences, Kerman, Iran. Electronic address:

The thermoalkalophilic lipase from Bacillus atrophaeus (BaL) was immobilized onto amine-functionalized graphene oxide nanosheets coated with the poly (maleic anhydride-alt-1-octadecene) copolymer (GO-NH-PMAO) and activated with glutaraldehyde as spacer arm through interfacial activation and subsequent multipoint covalent attachment. Experimental design method was applied for optimization of immobilization conditions including GO-NH-PMAO concentration, buffer concentration, pH, sonication time, enzyme concentration, glutaraldehyde concentration, time, and temperature. The optimum specific activity of the immobilized BaL (105.95 ± 2.37 U/mg) reached at 5 mg/mL for GO-NH-PMAO, 25 mM of buffer, pH 6.0, 60 min sonication time, 100 mM glutaraldehyde, 60 U/mL of enzyme, and 4 h of immobilization time at 25 °C, which was very close to the predicted amount (106.08 ± 1.42 U/mg). Maximum immobilization yield (81.35%) and efficiency (277.63%) were determined in optimal immobilization conditions. The obtained results clearly indicated that the immobilized BaL exhibited better stability at extreme temperature and pH than the free BaL. At temperature of 90 °C and pH 11, more than 90% of the initial activity of the immobilized BaL was retained. Furthermore, the immobilized BaL retained about 90% of its initial activity after 10 days of storage and 6 cycles of application. The esterification studies showed that maximum bioconversion of valeric acid to pentyl valerate using the free BaL (34.5%) and the immobilized BaL (96.3%) occurred in the xylene medium after 48 h of incubation at 60 °C. Therefore, the BaL immobilized on GO-NH-PMAO was introduced as an effective biocatalyst to synthesize green apple flavour ester.
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http://dx.doi.org/10.1016/j.ijbiomac.2020.08.101DOI Listing
November 2020

An Overview on Probiotics as an Alternative Strategy for Prevention and Treatment of Human Diseases.

Iran J Pharm Res 2019 ;18(Suppl1):31-50

Department of Medicine and epidemiology, School of veterinary Medicine, University of California, Davis, USA.

Probiotics are viable and useful microorganisms, which are beneficial factors for human and animal health by altering their microbial flora. Most of the probiotics belong to a large group of bacteria in the human gastrointestinal tract. There are several clinical shreds of evidence that show anti-carcinogenic effects of probiotics through altering digestive enzymes, inhibition of carcinogenic agents, and modulating the immune responses in experimental animals. Many studies have been performed to evaluate the potential effectiveness of probiotics in treating or preventing neurological diseases such as MS and novel treatment modality for T1D. The purpose of this study is to have an overview on probiotic microorganisms and to review the previous researches on the effects of probiotics on health through currently available literatures. The study was performed using following keywords; Probiotics, Cancer, Immune system, Multiple Sclerosis (MS) and Diabetes mellitus. PubMed/Medline, Clinicaltrials.gov, Ovid, Google Scholar, and Reaxcys databases used to find the full text of related articles. According to the current available data on probiotics and related health-promoting benefits, it seems that, consumption of probiotics can lead to the prevention and reduction the risk of cancer, diabetes, and multiple sclerosis. Although for the better and more decisive conclusion, there is a need to larger sample size clinical studies with more focus on the safety of these biological agents and their possible beneficial effects on different population.
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http://dx.doi.org/10.22037/ijpr.2020.112232.13620DOI Listing
http://www.ncbi.nlm.nih.gov/pmc/articles/PMC7393061PMC
January 2019

Osmolyte-Induced Folding and Stability of Proteins: Concepts and Characterization.

Iran J Pharm Res 2019 ;18(Suppl1):13-30

Department of Pharmaceutical Biotechnology, Faculty of Pharmacy, Tehran University of Medical Sciences, Tehran, Iran.

It is well-known that the typical protein's three-dimensional structure is relatively unstable in harsh conditions. A practical approach to maintain the folded state and thus improve the stability and activity of proteins in unusual circumstances is to directly apply stabilizing substances such as osmolytes to the protein-containing solutions. Osmolytes as natural occurring organic molecules typically called "compatible" solutes, based on the concept that they do not perturb cellular components. However, urea and guanidine hydrochloride (GuHCl) as denaturing osmolytes destabilize many macromolecular structures and inhibit functions. Several studies have been so far performed to explain the actual interaction of an osmolyte with a protein. The present review is aimed to achieve a collective knowledge of the progress arise in the field of osmolyte-protein interactions. The following is also an overview of the main techniques to measure protein stability in the presence of osmolytes.
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http://dx.doi.org/10.22037/ijpr.2020.112621.13857DOI Listing
http://www.ncbi.nlm.nih.gov/pmc/articles/PMC7393045PMC
January 2019

Design and synthesis of novel pyridazine N-aryl acetamides: In-vitro evaluation of α-glucosidase inhibition, docking, and kinetic studies.

Bioorg Chem 2020 09 6;102:104071. Epub 2020 Jul 6.

Drug Design and Development Research Center, The Institute of Pharmaceutical Sciences (TIPS), Tehran University of Medical Sciences, Tehran, Iran; Department of Medicinal Chemistry, Faculty of Pharmacy, Tehran University of Medical Sciences, Tehran, Iran. Electronic address:

We herein applied the four step-synthetic route to prepare the pyridazine core attached to the various N-aryl acetamides. By this approach, a new series of pyridazine-based compounds were synthesized, characterized and evaluated for their activities against α-glucosidase enzyme. In-vitro α-glucosidase assay established that twelve compounds are more potent than acarbose. Compound 7a inhibited α-glucosidase with the IC value of 70.1 µM. The most potent compounds showed no cytotoxicity against HDF cell line. Molecular docking and kinetic studies were performed to determine the modes of interaction and inhibition, respectively.
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http://dx.doi.org/10.1016/j.bioorg.2020.104071DOI Listing
September 2020

Synthesis, in vitro and in silico screening of 2-amino-4-aryl-6-(phenylthio) pyridine-3,5-dicarbonitriles as novel α-glucosidase inhibitors.

Bioorg Chem 2020 07 25;100:103879. Epub 2020 Apr 25.

Department of Pharmaceutical Biotechnology, Faculty of Pharmacy, Tehran University of Medical Sciences, Tehran, Iran.

Inhibition of α-glucosidase enzyme is of prime importance for the treatment of diabetes mellitus (DM). Apart of many organic scaffolds, pyridine based compounds have previously been reported for wide range of bioactivities. The current study reports a series of pyridine based synthetic analogues for their α-glucosidase inhibitory potential assessed by in vitro, kinetics and in silico studies. For this purpose, 2-amino-4-aryl-6-(phenylthio)pyridine-3,5-dicarbonitriles 1-28 were synthesized and subjected to in vitro screening. Several analogs, including 1-3, 7, 9, 11-14, and 16 showed many folds increased inhibitory potential in comparison to the standard acarbose (IC = 750 ± 10 µM). Interestingly, compound 7 (IC = 55.6 ± 0.3 µM) exhibited thirteen-folds greater inhibition strength than the standard acarbose. Kinetic studies on most potent molecule 7 revealed a competitive type inhibitory mechanism. In silico studies have been performed to examine the binding mode of ligand (compound 7) with the active site residues of α-glucosidase enzyme.
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http://dx.doi.org/10.1016/j.bioorg.2020.103879DOI Listing
July 2020

Design and synthesis of 4,5-diphenyl-imidazol-1,2,3-triazole hybrids as new anti-diabetic agents: in vitro α-glucosidase inhibition, kinetic and docking studies.

Mol Divers 2020 Mar 18. Epub 2020 Mar 18.

Endocrinology and Metabolism Research Center, Endocrinology and Metabolism Clinical Sciences Institute, Tehran University of Medical Sciences, Tehran, Iran.

Fourteen novel 4,5-diphenyl-imidazol-1,2,3-triazole hybrids 8a-n were synthesized with good yields by performing click reaction between the 4,5-diphenyl-2-(prop-2-yn-1-ylthio)-1H-imidazole and various benzyl azides. The synthesized compounds 8a-n were evaluated against yeast α-glucosidase, and all these compounds exhibited excellent inhibitory activity (IC values in the range of 85.6 ± 0.4-231.4 ± 1.0 μM), even much more potent than standard drug acarbose (IC = 750.0 μM). Among them, 4,5-diphenyl-imidazol-1,2,3-triazoles possessing 2-chloro and 2-bromo-benzyl moieties (compounds 8g and 8i) demonstrated the most potent inhibitory activities toward α-glucosidase. The kinetic study of the compound 8g revealed that this compound inhibited α-glucosidase in a competitive mode. Furthermore, docking calculations of these compounds were performed to predict the interaction mode of the synthesized compounds in the active site of α-glucosidase. A novel series of 4,5-diphenyl-imidazol-1,2,3-triazole hybrids 8a-n was synthesized with good yields by performing click reaction between the 4,5-diphenyl-2-(prop-2-yn-1-ylthio)-1Himidazole and various benzyl azides. The synthesized compounds 8a-n were evaluated against yeast α-glucosidase and all these compounds exhibited excellent inhibitory activity (IC50 values in the range of 85.6 ± 0.4-231.4 ± 1.0 μM), even much more potent than standard drug acarbose (IC50 = 750.0 μM).
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http://dx.doi.org/10.1007/s11030-020-10072-8DOI Listing
March 2020

Efficient Keratinolysis of Poultry Feather Waste by the Halotolerant Keratinase from Salicola Marasensis.

Iran J Pharm Res 2019 ;18(4):1862-1870

Department of Pharmaceutical Biotechnology, Faculty of Pharmacy, Tehran University of Medical Sciences, Tehran, Iran.

Sustainable development in the bio-treatment of large-scale biomass bulks requires high performance enzymes adapted to extreme conditions. An extracellular keratinolytic extract was obtained from the culture broth of a halotolerant strain of . Keratin hydrolyzing activity of the concentrated enzyme extract was observed on a 100 mg of pretreated feather waste. The concentrated enzyme was able to hydrolyze the poultry feathers by 25% after 12 h incubation. The bio-waste material was optimally hydrolyzed at pH 9 and temperature of 40 °C. Among reductants, 1,4-dithiothreitol, L-cysteine, 2-mercaptoethanol, glutathione, and sodium sulfate showed the most remarkable effect on the bio-waste keratinolysis, while the tested surfactants and urea had no significant effect on the keratinolytic activity. Hexane and hexadecane indicated strong effect on keratinase activity and bio-treatment in the presence of 1-butyl-3-methylimidazolium hexafluorophosphate ([BMIM][PF]) as a hydrophobic ionic liquid resulted in a maximal of 80% extraction yield of soluble proteins from feathers. Considering the stability of the extracellular keratinolytic content in [BMIM][PF], the observed keratinase activity was noteworthy suggesting that the secreted enzyme may contribute to the bioconversion of feather wastes.
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http://dx.doi.org/10.22037/ijpr.2019.111710.13312DOI Listing
http://www.ncbi.nlm.nih.gov/pmc/articles/PMC7059026PMC
January 2019

An efficient and targeted synthetic approach towards new highly substituted 6-amino-pyrazolo[1,5-a]pyrimidines with α-glucosidase inhibitory activity.

Sci Rep 2020 02 13;10(1):2595. Epub 2020 Feb 13.

Department of Medicinal Chemistry, Faculty of Pharmacy and The Institute of Pharmaceutical Sciences (TIPS), Tehran University of Medical Sciences, Tehran, Iran.

In an attempt to find novel α-glucosidase inhibitors, an efficient, straightforward reaction to synthesize a library of fully substituted 6-amino-pyrazolo[1,5-a]pyrimidines 3 has been investigated. Heating a mixture of α-azidochalcones 1 and 3-aminopyrazoles 2 under the mild condition afforded desired compounds with a large substrate scope in good to excellent yields. All obtained products were evaluated as α-glucosidase inhibitors and exhibited excellent potency with IC values ranging from 15.2 ± 0.4 µM to 201.3 ± 4.2 µM. Among them, compound 3d was around 50-fold more potent than acarbose (IC = 750.0 ± 1.5 µM) as standard inhibitor. Regarding product structures, kinetic study and molecular docking were carried out for two of the most potent ones.
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http://dx.doi.org/10.1038/s41598-020-59079-zDOI Listing
http://www.ncbi.nlm.nih.gov/pmc/articles/PMC7018746PMC
February 2020

Biodegradation of bisphenol A by the immobilized laccase on some synthesized and modified forms of zeolite Y.

J Hazard Mater 2020 03 23;386:121950. Epub 2019 Dec 23.

Department of Pharmaceutical Biotechnology, Faculty of Pharmacy, Tehran University of Medical Sciences, P.O. Box 14155-6451, Tehran, 1417614411, Iran. Electronic address:

Bisphenol A (BPA) is an environmental pollutant with adverse effects on different ecosystems. In this study, immobilized laccase enzymes onto inorganic supports were used to remove BPA. Laccase was successfully immobilized on sodium zeolite Y (NaY) and its modified desilicated (DSY) and dealuminated (DAY) forms. NaY-based supports were instrumentally characterized. The immobilized laccase on NaY (laccase@NaY), desilicated (laccase@DSY), and dealuminated (laccase@DAY) forms showed significant improvement on immobilization yield (IY%) and efficiency (IE%). Laccase@DSY and laccase@NaY showed IY% = 73.18 ± 3.33 % and 46.23 ± 1.81 % and IE% = 94.50 ± 1.86 %, and 74.39 ± 1.41 %, respectively, whereas IY% and IE% for laccase@DAY were achieved as 81.12 ± 1.32 % and 98.56 ± 2.93 %, respectively. The supports also increased the enzyme characteristics such as pH-temperature range, catalytic stability, and reusability. K values were 0.73 ± 0.05, 0.26 ± 0.09, 0.31 ± 0.5, and 1.01 ± 0.03 mM for laccase@NaY, laccase@DAY, laccase@DSY, and the free enzyme, respectively. The enzyme demonstrated higher biodegradation ability of bisphenol A upon immobilization on the supports compared to that of the soluble enzyme. A bio-removal yield of 86.7 % was obtained considering three parameters including amount of laccase@DAY (8 U mg), concentration of BPA (0.5 mM), and treatment time (1 h) based on response surface methodology (RSM). Biodegradation metabolites (49 ± 5.8 %) and unconverted BPA (14 ± 5.2 %) were analyzed by gas chromatography-mass spectrometry.
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http://dx.doi.org/10.1016/j.jhazmat.2019.121950DOI Listing
March 2020

Synthesis and biological evaluation of new benzimidazole-1,2,3-triazole hybrids as potential α-glucosidase inhibitors.

Bioorg Chem 2020 01 4;95:103482. Epub 2019 Dec 4.

Nano Alvand Company, Avicenna Tech Park, Tehran University of Medical Sciences, Tehran 1439955991, Iran. Electronic address:

In this study, a series of benzimidazole-1,2,3-triazole hybrids 8a-n as new α-glucosidase inhibitors were designed and synthesized. In vitro α-glucosidase inhibition activity results indicated that all the synthesized compounds (IC values ranging from 25.2 ± 0.9 to 176.5 ± 6.7 μM) exhibited more inhibitory activity in comparison to standard drug acarbose (IC = 750.0 ± 12.5 μM). Enzyme kinetic study on the most potent compound 8c revealed that this compound was a competitive inhibitor into α-glucosidase. Moreover, the docking study was performed in order to evaluation of interaction modes of the synthesized compounds in the active site of α-glucosidase and to explain structure-activity relationships of the most potent compounds and their corresponding analogs.
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http://dx.doi.org/10.1016/j.bioorg.2019.103482DOI Listing
January 2020

Immobilization of Thermoalkalophilic Lipase from Bacillus atrophaeus FSHM2 on Amine-Modified Graphene Oxide Nanostructures: Statistical Optimization and Its Application for Pentyl Valerate Synthesis.

Appl Biochem Biotechnol 2020 Jun 10;191(2):579-604. Epub 2019 Dec 10.

Department of Pharmaceutical Biotechnology, Faculty of Pharmacy, Kerman University of Medical Sciences, Kerman, Iran.

Synthesis of (3-aminopropyl) triethoxysilane (APTES)-functionalized graphene oxide (GO) nanosheets, statistical optimization of conditions for immobilization of Bacillus atrophaeus lipase (BaL) on as-synthesized support, and application of the immobilized BaL for esterification of valeric acid were carried out in this investigation. The optimum specific activity of the immobilized BaL (81.60 ± 0.28 U mg) was achieved at 3 mg mL of GO-NH, 50 mM of phosphate buffer, pH 7.0, 60 min sonication time, 100 mM glutaraldehyde, 25 U mL of enzyme, and 8 h immobilization time at 4 °C. The immobilized BaL retained about 90% of its initial activity after 10 days of storage. Moreover, about 70% of the initial activity of the immobilized BaL was retained after 10 cycles of application. The results of esterification studies exhibited that maximum pentyl valerate synthesis using the free BaL (34.5%) and the immobilized BaL (92.7%) occurred in the organic solvent medium (xylene) after 48 h of incubation at 60 °C.
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http://dx.doi.org/10.1007/s12010-019-03180-1DOI Listing
June 2020

Study on the interaction of 1,5-diaryl pyrrole derivatives with α-glucosidase; synthesis, molecular docking, and kinetic study.

Med Chem 2019 Dec 5. Epub 2019 Dec 5.

Department of Medicinal Chemistry, Faculty of Pharmacy, Drug Design and Development Research Center and The Institute of Pharmaceutical Sciences (TIPS), Tehran University of Medical Sciences, Tehran. Iran.

Background: The delaying of absorption of glucose is one of the principal therapeutic approaches of type 2 diabetes. α-glucosidase inhibitors compete with the α-glucosidase enzyme activity, which helps to reduce the conversion of carbohydrates into glucose and thereby control the postprandial hyperglycemia incidence.

Objective: The aim of this study was to synthesize a series of novel 1,5-diphenyl pyrrole derivatives and evaluate their in vitro α-glucosidase inhibitory activities.

Methods: Compounds were synthesized through a multistep reaction and were evaluated for α-glucosidase inhibitory activities. Molecular docking and kinetic studies were carried out to predict the mode of binding and mechanism of inhibition for the most active compounds, 5g and 5b, against α-glucosidase.

Results: Synthesized compounds showed good in vitro α-glucosidase inhibitory activity with IC50 values in the range of (117.5 ± 3.8 to 426.0 ± 10.2 µM) as compared to acarbose, the standard drug, (750 ± 8.7 µM). Compound 5g (117.5 ± 3.8 µM) ascertained as the most potent inhibitor of α-glucosidase in a competitive mode. The binding energies of compounds 5g and 5b (119.0 ± 7.5 µM), as observed from the best docking conformations, indicates that they have a lower free binding energy (-3.26 kcal/mol and -3.0 kcal/mol, respectively) than acarbose (2.47 kcal/mol).

Conclusion: The results of our study reveal that the synthesized compounds are a potential candidate for α-glucosidase inhibitors for the management of postprandial hyperglycemia for further investigation.
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http://dx.doi.org/10.2174/1573406415666191206100336DOI Listing
December 2019

Photocatalytic degradation of ketoconazole by Z-scheme AgPO/graphene oxide: response surface modeling and optimization.

Environ Sci Pollut Res Int 2020 Jan 30;27(1):250-263. Epub 2019 Nov 30.

Biomaterials Group, The Institute of Pharmaceutical Sciences (TIPS), Tehran University of Medical Sciences, Tehran, Iran.

Ketoconazole is an imidazole fungicide which is commonly used as pharmaceutical and healthcare products. Residual amount of this compound can cause adverse ecological health problems. The present study investigated ketoconazole photocatalytic degradation using AgPO/graphene oxide (GO). AgPO/GO and AgPO as visible light-driven photocatalysts was synthesized using the in situ growth method. Degradation of ketoconazole at the concentration of 1-20 mg/L in aqueous solutions was optimized in the presence of AgPO/GO nanocomposite with the dosage of 0.5-2 g/L, contact time of 15-20 min, and pH of 5-9 using response surface methodology. A second-order model was selected as the best fitted model with R value and lack of fit as 0.935 and 0.06, respectively. Under the optimized conditions, the AgPO/GO catalyst achieved a photocatalytic efficiency of 96.53% after 93.34 min. The photocatalytic activity, reaction kinetics, and stability were also investigated. The results indicated that the AgPO/GO nanocomposite exhibited higher photocatalytic activity for ketoconazole degradation, which was 2.4 times that of pure AgPO. Finally, a direct Z-scheme mechanism was found to be responsible for enhanced photocatalytic activity in the AgPO/GO nanocomposite. The high photocatalytic activity, acceptable reusability, and good aqueous stability make the AgPO/GO nanocomposite a promising nanophotocatalyst for photocatalytic degradation of azoles contaminants.
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http://dx.doi.org/10.1007/s11356-019-06812-5DOI Listing
January 2020

Purification and study of anti-cancer effects of serralysin.

Iran J Microbiol 2019 Aug;11(4):320-327

Department of Drug and Food Control, School of Pharmacy, Tehran University of Medical Sciences, Tehran, Iran.

Background And Objectives: Serralysin is an extracellular metalloprotease from which has been the subject of extensive biological investigations. The goal of this study was to extract and purify serralysin from and to investigate its cytotoxic activity on the colorectal cancer cell line.

Materials And Methods: The presence of the serralysin gene was confirmed using PCR. The supernatant of bacterial culture was collected and precipitated using ammonium sulfate. The precipitated protein was dialyzed and subjected to ion exchange chromatography for further purification. Casein assay and skim milk assay was used to confirm the enzymatic activity. SDS-PAGE was used to visualize the presence of serralysin. Metalloprotease inhibition activity was performed using 50 mM EDTA. Cytotoxic activity of serralysin was assessed on MTT assay.

Results: The PCR product corresponding to serralysin was estimated to be approximately 1500 bp. A transparent zone around the bacterial colonies on skim milk agar and casein digestion confirmed the proteolytic activity of serralysin. A 52 kDa band in SDS-PAGE corresponding to serralysin was observed before and after purification processes. MTT assay showed IC values 24.78 μg/ml and 19.16 μg/ml after 24 h and 48 h exposure of Caco-2 cells to serralysin, respectively.

Conclusion: Our results showed that native serralysin has anticancer potential and may be a candidate for further pharmaceutical research and development. Further and mechanistic studies are suggested to confirm the biological activities.
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http://www.ncbi.nlm.nih.gov/pmc/articles/PMC6829104PMC
August 2019

Design, synthesis, in vitro, and in silico studies of novel diarylimidazole-1,2,3-triazole hybrids as potent α-glucosidase inhibitors.

Bioorg Med Chem 2019 12 15;27(23):115148. Epub 2019 Oct 15.

Department of Medicinal Chemistry, Faculty of Pharmacy, Tehran University of Medical Sciences, Tehran, Iran; Persian Medicine and Pharmacy Research Center, Faculty of Pharmacy, Tehran University of Medical Sciences, Tehran, Iran. Electronic address:

In this work, new derivatives of diarylimidazole-1,2,3-triazole 7a-p were designed, synthesized, and evaluated for their in vitro α-glucosidase inhibitory activity. All compounds showed potent inhibitory activity in the range of IC = 90.4-246.7 µM comparing with acarbose as the standard drug (IC = 750.0 µM). Among the synthesized compounds, compounds 7b, 7c, and 7e were approximately 8 times more potent than acarbose. The kinetic study of those compounds indicated that they acted as the competitive inhibitors of α-glucosidase. Molecular docking studies were also carried out for compounds 7b, 7c, and 7e using modeled α-glucosidase to find the interaction modes responsible for the desired inhibitory activity.
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http://dx.doi.org/10.1016/j.bmc.2019.115148DOI Listing
December 2019

Biomedical and Pharmaceutical-Related Applications of Laccases.

Curr Protein Pept Sci 2020 ;21(1):78-98

Department of Pharmaceutical Biotechnology, Faculty of Pharmacy, Tehran University of Medical Sciences, P.O. Box 14155-6451, Tehran 1417614411, Iran.

The oxidation of a vast range of phenolic and non-phenolic substrates has been catalyzed by laccases. Given a wide range of substrates, laccases can be applied in different biotechnological applications. The present review was conducted to provide a broad context in pharmaceutical- and biomedical- related applications of laccases for academic and industrial researchers. First, an overview of biological roles of laccases was presented. Furthermore, laccase-mediated strategies for imparting antimicrobial and antioxidant properties to different surfaces were discussed. In this review, laccase-mediated mechanisms for endowing antimicrobial properties were divided into laccase-mediated bio-grafting of phenolic compounds on lignocellulosic fiber, chitosan and catheters, and laccase-catalyzed iodination. Accordingly, a special emphasis was placed on laccase-mediated functionalization for creating antimicrobials, particularly chitosan-based wound dressings. Additionally, oxidative bio-grafting and oxidative polymerization were described as the two main laccase-catalyzed reactions for imparting antioxidant properties. Recent laccase-related studies were also summarized regarding the synthesis of antibacterial and antiproliferative agents and the degradation of pharmaceuticals and personal care products.
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http://dx.doi.org/10.2174/1389203720666191011105624DOI Listing
January 2021

Coumarin-based Scaffold as α-glucosidase Inhibitory Activity: Implication for the Development of Potent Antidiabetic Agents.

Mini Rev Med Chem 2020 ;20(2):134-151

Department of Medicinal Chemistry, Faculty of Pharmacy, Drug Design and Development Research Center and The Institute of Pharmaceutical Sciences (TIPS), Tehran University of Medical Sciences, Tehran, Iran.

Background: Delaying the absorption of glucose through α-glucosidase enzyme inhibition is one of the therapeutic approaches in the management of Type 2 diabetes, which can reduce the incidence of postprandial hyperglycemia. The existence of chronic postprandial hyperglycemia impaired the endogenous antioxidant defense by inducing oxidative stress-induced pancreatic β-cell destruction through uncontrolled generation of free radicals such as ROS, which in turn, leads to various macrovascular and microvascular complications. The currently available α -glucosidase inhibitors, for instance, acarbose, have some side effects such as hypoglycemia at higher doses, liver problems, meteorism, diarrhea, and lactic acidosis. Therefore, there is an urgent need to discover and develop potential α-glucosidase inhibitors.

Objective: Based on suchmotifs, researchers are intrigued to search for the best scaffold that displays various biological activities. Among them, coumarin scaffold has attracted great attention. The compound and its derivatives can be isolated from various natural products and/or synthesized for the development of novel α-glucosidase inhibitors.

Results: This study focused on coumarin and its derivatives as well as on their application as potent antidiabetic agents and has also concentrated on the structure-activity relationship.

Conclusion: This review describes the applications of coumarin-containing derivatives as α - glucosidase inhibitors based on published reports which will be useful for innovative approaches in the search for novel coumarin-based antidiabetic drugs with less toxicity and more potency.
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http://dx.doi.org/10.2174/1389557519666190925162536DOI Listing
October 2020