Sarkar Ankita, Sengupta Kushal, Chatterjee Sudipta, Seal Manas, Faller Peter, Dey Somdatta Ghosh, Dey Abhishek
Department of Inorganic Chemistry, Indian Association for the Cultivation of Science, 2A & 2B Raja S.C. Mullick Road, Kolkata 700032, India.
Biometals and Biology Chemistry, Institut de Chemie (CNRS UMR 7177), University of Strasbourg, 4 rue B. pascal, 67081 Strasbourg Cedex, France.
ACS Omega. 2018 Oct 25;3(10):13994-14003. doi: 10.1021/acsomega.8b01736. eCollection 2018 Oct 31.
Aβ(1-40) peptide is mutated to introduce cysteine residue to allow formation of organized self-assembled monolayers (SAMs) on Au electrodes. Three mutants of this peptide are produced, which vary in the position of the inserted cysteine residue. Fourier transform infrared data on these peptide SAMs show the presence of both α helices and β sheet in these Aβ constructs. These peptide constructs interact with cytochrome (Cyt), allowing electron transfer between Cyt and the electrode via the Aβ peptides. Binding of metals like Zn or Cu induces changes in the morphologies of these assemblies, making them fold, which inhibits their spontaneous interaction with Cyt.
Aβ(1-40)肽发生突变以引入半胱氨酸残基，从而在金电极上形成有序的自组装单分子层（SAMs）。制备了该肽的三种突变体，其插入的半胱氨酸残基位置不同。这些肽SAMs的傅里叶变换红外数据表明，在这些Aβ构建体中同时存在α螺旋和β折叠。这些肽构建体与细胞色素（Cyt）相互作用，使得电子能够通过Aβ肽在Cyt和电极之间转移。锌或铜等金属的结合会引起这些组装体形态的变化，使其折叠，从而抑制它们与Cyt的自发相互作用。
