Aromatic ‐interaction‐mediated inhibition of β‐amyloid assembly structures and cytotoxicity
This study could be beneficial for developing peptide‐based inhibitory agents for amyloidoses. Copyright © 2017 European Peptide Society and John Wiley & Sons, Ltd.
We demonstrate the inhibitory effect of oligomeric polypeptides containing representative aromatic amino acids of tryptophan and tyrosine (K8Y8, K4Y8, K8W8) on Aβ42 fibrillization process. Through direct binding at the N‐terminus of Aβ42 by π–π stacking between aromatic amino acids and Phe19, together with hydrogen bonds, the polypeptides can remarkably weaken the aggregation and fibrillization process of Aβ42, inhabit the β‐sheet formation of Aβ42, and reduce the cytotoxicity of S‐SY5Y cells.
Source: Journal of Peptide Science - Category: Biochemistry Authors: Hanyi Xie, Jiaxi Peng, Changliang Liu, Xiaocui Fang, Hongyang Duan, Yimin Zou, Yanlian Yang, Chen Wang Tags: Research Article Source Type: research