5 results match your criteria assemblies cross-sequence

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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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Experimental and Computational Protocols for Studies of Cross-Seeding Amyloid Assemblies.

Methods Mol Biol 2018 ;1777:429-447

Department of Chemical & Biomolecular Engineering, The University of Akron, Akron, OH, USA.

Alzheimer's disease (AD) and type 2 diabetes (T2D) are two common protein aggregation diseases. Compelling evidence has shown a link between AD and T2D, which may derive from interspecies cross-sequence interactions between amyloid-β peptide (Aβ), associated with AD, and human islet amyloid polypeptide (hIAPP), associated with T2D. Herein, we present experimental and computational protocols and tools to study the aggregate structures and kinetics, conformational conversion, and molecular interactions of Aβ-hIAPP mixtures. Read More

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February 2019

Polymorphic Associations and Structures of the Cross-Seeding of Aβ1-42 and hIAPP1-37 Polypeptides.

J Chem Inf Model 2015 Aug 24;55(8):1628-39. Epub 2015 Jul 24.

Department of Geriatric Neurology, Nanjing Brain Hospital Affiliated to Nanjing Medical University , Nanjing, Jiangsu 210029, China.

Emerging evidence have shown that the patients with Alzheimer's disease (AD) often have a higher risk of later developing type II diabetes (T2D), and vice versa, suggesting a potential pathological link between AD and T2D. Amyloid-β (Aβ) and human islet amyloid polypeptide (hIAPP) are the principle causative components responsible for the pathologies of AD and T2D, respectively. The cross-sequence interactions between Aβ and hIAPP may provide a molecular basis for better understanding the potential link between AD and T2D. Read More

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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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Structural and energetic insight into the cross-seeding amyloid assemblies of human IAPP and rat IAPP.

J Phys Chem B 2014 Jun 12;118(25):7026-36. Epub 2014 Jun 12.

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

The misfolding and aggregation of human islet amyloid polypeptide (hIAPP or amylin) into small oligomers and large amyloid fibrils is believed to be responsible for the dysfunction and death of pancreatic β-cells in diabetes type II. However, rat IAPP (rIAPP), which differs from the hIAPP by only 6 of 37 residues, lacks the ability to form amyloid fibrils and to induce cell death. Little is known about the cross-sequence interactions and cross-seeding structures between hIAPP and rIAPP peptides. Read More

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