Molecular Tethering Effect of C-Terminus of Amyloid Peptide A尾42
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- 作者：Lei Liu ; Lin Niu ; Meng Xu ; Qiusen Han ; Hongyang Duan ; Mingdong Dong ; Flemming Besenbacher ; Chen Wang ; Yanlian Yang
- 刊名：ACS Nano
- 出版年：2014
- 出版时间：September 23, 2014
- 年：2014
- 卷：8
- 期：9
- 页码：9503-9510
- 全文大小：510K
- ISSN：1936-086X
文摘
Amyloid peptides are considered to be the main contributor for the membrane disruption related to the pathogenesis of degenerative diseases. The variation of amino acids at the carboxylic terminus of amyloid peptide has revealed significant effects on the modulation of abnormal assemblies of amyloid peptides. In this work, molecular binding agents were tethered to the C-terminus of 尾-amyloid peptide 1鈥?2 (A尾42). The molecular interaction between A尾42 and molecule tethers was identified at single molecule level by using scanning tunneling microscopy (STM). The mechanistic insight into the feature variation of the self-assembly of A尾42 peptide caused by molecular tethering at C-terminus was clearly revealed, which could appreciably affect the nucleation of amyloid peptide, thus reducing the membrane disruptions.