Helix Dipole and Membrane Electrostatics Delineate Conformational Transitions in the Self-Assembly of Amyloidogenic Peptides
Author:
Affiliation:
1. Carlson School of Chemistry and Biochemistry, Clark University, 950 Main Street, Worcester, Massachusetts 01610, United States
Funder
U.S. Department of Health and Human Services
Publisher
American Chemical Society (ACS)
Subject
Electrochemistry,Spectroscopy,Surfaces and Interfaces,Condensed Matter Physics,General Materials Science
Link
https://pubs.acs.org/doi/pdf/10.1021/acs.langmuir.0c00723
Reference69 articles.
1. The Interplay of Catalysis and Toxicity by Amyloid Intermediates on Lipid Bilayers: Insights from Type II Diabetes
2. Membrane Disruption and Early Events in the Aggregation of the Diabetes Related Peptide IAPP from a Molecular Perspective
3. How Do Membranes Initiate Alzheimer’s Disease? Formation of Toxic Amyloid Fibrils by the Amyloid β-Protein on Ganglioside Clusters
4. Membrane interactions of intrinsically disordered proteins: The example of alpha-synuclein
5. Structure and dynamics of the extended-helix state of alpha-synuclein: Intrinsic lability of the linker region
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