Computational investigation of the binding of a designed peptide to λ light chain amyloid fibril-Reference-Cited by-同舟云学术

Computational investigation of the binding of a designed peptide to λ light chain amyloid fibril

Published:2021 Issue:36 Volume:23 Page:20634-20644
ISSN:1463-9076
Container-title:Physical Chemistry Chemical Physics
language:en
Short-container-title:Phys. Chem. Chem. Phys.

Author:

Wang Zhenyu¹^ORCID,Huang Wanying¹,Liu Manjun²,Kennel Stephen J³,Wall Jonathan S³,Cheng Xiaolin⁴

Affiliation:

1. T-Life Research Center, State Key Laboratory of Surface Physics, Department of Physics, Fudan University, Shanghai 200433, China

2. College of Information Engineering, Eastern Liaoning University, Dandong City, Liaoning Province 118003, China

3. Department of Medicine, The University of Tennessee Medical Center, Knoxville, TN, 37920, USA

4. Division of Medicinal Chemistry and Pharmacognosy, College of Pharmacy, and Translational Data Analytics Institute, The Ohio State University, Columbus, OH, 43210, USA

Abstract

Peptide P62 only binds to the canonical interface of the amyloid fibril. Lysine residues of P62 play an important role in the binding process by forming initial contacts with aspartic acids on the fibril surface.

Funder

Ohio State University

Fudan University

Publisher

Royal Society of Chemistry (RSC)

Subject

Physical and Theoretical Chemistry,General Physics and Astronomy

Link

http://pubs.rsc.org/en/content/articlepdf/2021/CP/D1CP01825F

Reference52 articles.

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5. Thermodynamic Instability of Human λ6 Light Chains: Correlation with Fibrillogenicity

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