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Protein nanofibril design via manipulation of hydrogen bonds

Chemistry

Protein nanofibril design via manipulation of hydrogen bonds

N. Aggarwal, D. Eliaz, et al.

This innovative study reveals how the manipulation of hydrogen bonds in amyloidogenic peptides can significantly alter fibril morphology, structure, and nanomechanical properties. Discover insights into the intricate molecular interactions that shape protein supramolecular constructs, conducted by Nidhi Aggarwal, Dror Eliaz, Hagai Cohen, Irit Rosenhek-Goldian, Sidney R. Cohen, Anna Kozell, Thomas O. Mason, and Ulyana Shimanovich.

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Playback language: English
Abstract
Amyloid nanofibril formation is crucial in both natural materials (e.g., silk) and degenerative diseases. This study investigates whether manipulating hydrogen bonds (H-bonds) in amyloidogenic peptides alters their fibrillation. Tailored H-bond network changes minimally affect initial nucleation but significantly alter higher-level network packaging, leading to variations in fibril morphology, structure, and nanomechanical properties. This enhances understanding of molecular interactions' role in shaping protein supramolecular constructs.
Publisher
Communications Chemistry
Published On
May 11, 2021
Authors
Nidhi Aggarwal, Dror Eliaz, Hagai Cohen, Irit Rosenhek-Goldian, Sidney R. Cohen, Anna Kozell, Thomas O. Mason, Ulyana Shimanovich
Tags
amyloid nanofibrils
hydrogen bonds
fibrillation
peptides
molecular interactions
fibril morphology

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