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Monomer-targeting affinity peptide inhibitors of amyloid with no self-fibrillation and low cytotoxicity

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Abstract

We utilized solution-phase biopanning to obtain a de novo peptide (LA12) that specifically bound to the core region of the human amylin monomer. LA12 stabilized the random coil conformation of amylin to suppress aggregation in a dose-dependent manner with the highest suppression effect of 78% and reduced the cytotoxicity of amylin.

Graphical abstract: Monomer-targeting affinity peptide inhibitors of amyloid with no self-fibrillation and low cytotoxicity

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Article information


Submitted
06 Nov 2019
Accepted
07 Jan 2020
First published
08 Jan 2020

Chem. Commun., 2020, Advance Article
Article type
Communication

Monomer-targeting affinity peptide inhibitors of amyloid with no self-fibrillation and low cytotoxicity

Q. Xuan, J. He, M. Li, R. Chai, C. Wang, Y. Wang and P. Wang, Chem. Commun., 2020, Advance Article , DOI: 10.1039/C9CC08671D

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