<i>De novo</i> amyloid peptides with subtle sequence variations differ in their self-assembly and nanomechanical properties-Reference-Cited by-同舟云学术

De novo amyloid peptides with subtle sequence variations differ in their self-assembly and nanomechanical properties

Published:2023 Issue:27 Volume:19 Page:5150-5159
ISSN:1744-683X
Container-title:Soft Matter
language:en
Short-container-title:Soft Matter

Author:

Abernathy Hannah G.¹^ORCID,Saha Jhinuk²,Kemp Lisa K.¹,Wadhwani Parvesh³^ORCID,Clemons Tristan D.¹,Morgan Sarah E.¹^ORCID,Rangachari Vijayaraghavan²⁴^ORCID

Affiliation:

1. School of Polymer Science & Engineering, University of Southern Mississippi, Hattiesburg, MS, USA

2. Department of Chemistry and Biochemistry, School of Mathematics and Natural Sciences, University of Southern Mississippi, Hattiesburg, MS, USA

3. Department of Molecular Biophysics (IBG 2), Karlsruhe Institute of Technology (KIT), Hermann-von-Helmholtz-Platz 1, 76344, Karlsruhe, Germany

4. Center for Molecular and Cellular Biosciences, University of Southern Mississippi, Hattiesburg, MS, USA

Abstract

Proteinaceous amyloids are well known for their widespread pathological roles but lately have emerged also as key components in several biological functions.

Funder

National Science Foundation

Publisher

Royal Society of Chemistry (RSC)

Subject

Condensed Matter Physics,General Chemistry

Link

http://pubs.rsc.org/en/content/articlepdf/2023/SM/D3SM00604B

Reference55 articles.

1. The Amyloid State of Proteins in Human Diseases

2. Prion-like C-Terminal Domain of TDP-43 and α-Synuclein Interact Synergistically to Generate Neurotoxic Hybrid Fibrils

3. Molecular Mechanisms of TDP-43 Misfolding and Pathology in Amyotrophic Lateral Sclerosis

4. Biophysical characteristics of lipid‐induced Aβ oligomers correlate to distinctive phenotypes in transgenic mice

5. Islet Amyloid Polypeptide: Structure, Function, and Pathophysiology

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