National Center for Nanoscience and Technology , Beijing 100190, China.
ACS Nano. 2014 Sep 23;8(9):9503-10. doi: 10.1021/nn503737r. Epub 2014 Sep 10.
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 β-amyloid peptide 1-42 (Aβ42). The molecular interaction between Aβ42 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 Aβ42 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.
淀粉样肽被认为是与退行性疾病发病机制相关的膜破坏的主要贡献者。在淀粉样肽的羧基末端的氨基酸变化已经揭示了对淀粉样肽异常聚集的调节有显著影响。在这项工作中，分子结合剂被连接到β-淀粉样肽 1-42（Aβ42）的 C 末端。通过使用扫描隧道显微镜（STM）在单分子水平上鉴定了 Aβ42 和分子连接之间的分子相互作用。在 C 末端通过分子连接对 Aβ42 肽自组装的特征变化的机制见解被清楚地揭示出来，这可以显著影响淀粉样肽的成核，从而减少膜破坏。
