Acidic pH Promotes Refolding and Macroscopic Assembly of Amyloid β (16–22) Peptides at the Air

Acidic pH Promotes Refolding and Macroscopic Assembly of Amyloid β (16–22) Peptides at the Air–Water Interface

Published:2022-07-15 Issue:29 Volume:13 Page:6674-6679
ISSN:1948-7185
Container-title:The Journal of Physical Chemistry Letters
language:en
Short-container-title:J. Phys. Chem. Lett.

Author:

Lu Hao¹^ORCID,Bellucci Luca²,Sun Shumei³,Qi Daizong¹,Rosa Marta⁴⁵^ORCID,Berger Rüdiger¹^ORCID,Corni Stefano⁴⁵^ORCID,Bonn Mischa¹^ORCID

Affiliation:

1. Max Planck Institute for Polymer Research, Ackermannweg 10, 55128 Mainz, Germany

2. NEST − Istituto di Nanoscienze del Consiglio Nazionale delle Ricerche CNR-NANO and Scuola Normale Superiore, Piazza S. Silvestro 12, Pisa, 56127, Italy

3. Department of Physics and Applied Optics Beijing Area Major Laboratory, Beijing Normal University, Beijing, 100875, China

4. Istituto di Nanoscienze del Consiglio Nazionale delle Ricerche CNR-NANO, 41125 Modena, Italy

5. Dipartimento di Scienze Chimiche, Università di Padova, 35131 Padova, Italy

Funder

Max-Planck-Gesellschaft

Publisher

American Chemical Society (ACS)

Subject

General Materials Science,Physical and Theoretical Chemistry

Link

https://pubs.acs.org/doi/pdf/10.1021/acs.jpclett.2c01171

Reference40 articles.

1. Protein Misfolding, Functional Amyloid, and Human Disease

2. The amyloid cascade hypothesis for Alzheimer's disease: an appraisal for the development of therapeutics

3. The Polyphenol EGCG Inhibits Amyloid Formation Less Efficiently at Phospholipid Interfaces than in Bulk Solution

4. Morphology and Persistence Length of Amyloid Fibrils Are Correlated to Peptide Molecular Structure

5. Chiral Sum Frequency Generation Spectroscopy for Characterizing Protein Secondary Structures at Interfaces

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