5 results match your criteria cross-sequence interaction

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Amyloid cross-sequence interaction between Aβ(1-40) and αA(66-80) in relation to the pathogenesis of cataract.

Int J Biol Macromol 2021 May 21;179:61-70. Epub 2021 Feb 21.

Ulm University, Institute of Protein Biochemistry, Helmholtzstraße 8/1, 89081 Ulm, Germany; Department of Biotechnology, Central University of Rajasthan, NH-8 Bandarsindri, Kishangarh, Ajmer 305817, Rajasthan, India. Electronic address:

Alzheimer's disease (AD) and cataract represent two common protein misfolding diseases closely associated with aging. Growing evidence suggests that these two diseases may be interrelated with each other through cross-sequence interactions between β-amyloid (Aβ) peptide and the short aggregating peptides derived from proteolytic breakdown of α-crystallin. αΑ(66-80) is one of several peptides produced by the proteolytic breakdown of α-crystallin in aged eye lens. Read More

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Cross-Seeding Interaction between β-Amyloid and Human Islet Amyloid Polypeptide.

ACS Chem Neurosci 2015 Oct 17;6(10):1759-68. Epub 2015 Aug 17.

Department of Chemical and Biomolecular Engineering, The University of Akron , Akron, Ohio 44325, United States.

Alzheimer's disease (AD) and type 2 diabetes (T2D) are two common protein misfolding diseases. Increasing evidence suggests that these two diseases may be correlated with each other via cross-sequence interactions between β-amyloid peptide (Aβ) associated with AD and human islet amyloid polypeptide (hIAPP) associated with T2D. However, little is known about how these two peptides work and how they interact with each other to induce amyloidogenesis. Read More

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October 2015

Interfacial interaction and lateral association of cross-seeding assemblies between hIAPP and rIAPP oligomers.

Phys Chem Chem Phys 2015 Apr;17(16):10373-82

Department of Chemical and Biomolecular Engineering, The University of Akron, Akron, Ohio 44325, USA.

Cross-sequence interactions between different amyloid peptides are important not only for the fundamental understanding of amyloid aggregation and polymorphism mechanisms, but also for probing a potential molecular link between different amyloid diseases. Here, we computationally modeled and simulated a series of hybrid hIAPP (human islet amyloid polypeptide)-rIAPP (rat islet amyloid polypeptide) assemblies and probed their structural stability, lateral association, and interfacial interactions using combined peptide-packing search, molecular dynamics (MD) simulations, and the Monte Carlo sampling method. We then identified a number of stable and highly populated hIAPP-rIAPP assemblies at the lowest energy states, in which hIAPP and rIAPP oligomers were stacked laterally on top of each other to form supramolecular β-sheet double layers in an antiparallel fashion. Read More

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Cross-sequence interactions between human and rat islet amyloid polypeptides.

Langmuir 2014 May 1;30(18):5193-201. Epub 2014 May 1.

Department of Chemical and Biomolecular Engineering, The University of Akron , Akron, Ohio 44325, United States.

Human islet amyloid polypeptide (hIAPP) can assemble into toxic oligomers and fibrils, which are associated with cell degeneration and the pathogenesis of type 2 diabetes. Cross-interaction of hIAPP with rat IAPP (rIAPP)--a non-amyloidogenic peptide with high sequence similarity to hIAPP--might influence the aggregation and toxicity of hIAPP. However, the exact role of rIAPP in hIAPP aggregation and toxicity still remains unclear. Read More

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In silico cross seeding of Aβ and amylin fibril-like oligomers.

ACS Chem Neurosci 2013 Nov 19;4(11):1488-500. Epub 2013 Sep 19.

Department of Chemistry & Biochemistry, University of Oklahoma , Norman, Oklahoma 73019, United States.

Recent epidemiological data have shown that patients suffering from Type 2 Diabetes Mellitus have an increased risk to develop Alzheimer's disease and vice versa. A possible explanation is the cross-sequence interaction between Aβ and amylin. Because the resulting amyloid oligomers are difficult to probe in experiments, we investigate stability and conformational changes of Aβ-amylin heteroassemblies through molecular dynamics simulations. Read More

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November 2013
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