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Methods Mol Biol. 2018;1777:429-447. doi: 10.1007/978-1-4939-7811-3_27.

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

Author information

1
Department of Chemical & Biomolecular Engineering, The University of Akron, Akron, OH, USA.
2
College of Life Sciences and Chemistry Hunan University of Technology, Zhuzhou, China.
3
College of Chemical and Biological Engineering, Zhejiang University, Zhejiang, Hangzhou, China.
4
State Key Laboratory of Pollution Control and Resource Reuse, School of Environmental Science and Engineering, Tongji University, Shanghai, China.
5
Basic Science Program, Leidos Biomedical Research, Inc., Cancer and Inflammation Program, National Cancer Institute, Frederick, MD, USA.
6
Basic Science Program, Leidos Biomedical Research, Inc., Cancer and Inflammation Program, National Cancer Institute, Frederick, MD, USA. nussinor@helix.nih.gov.
7
Sackler Institute of Molecular Medicine, Department of Human Genetics and Molecular Medicine Sackler School of Medicine, Tel Aviv University, Tel Aviv, Israel. nussinor@helix.nih.gov.
8
Department of Chemical & Biomolecular Engineering, The University of Akron, Akron, OH, USA. zhengj@uakron.edu.

Abstract

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. These protocols could be generally applied to other cross-seeding behaviors of amyloid peptides.

KEYWORDS:

Alzheimer disease; Amyloid peptides; Aβ; Cross-seeding; Diabetes; hIAPP

PMID:
29744852
PMCID:
PMC6456059
DOI:
10.1007/978-1-4939-7811-3_27
[Indexed for MEDLINE]
Free PMC Article

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