三肽
部分
化学
自组装
肽
立体化学
水溶液中的金属离子
酪氨酸
芳香性
组合化学
金属
结晶学
分子
有机化学
生物化学
作者
Narendra Singh,Ramesh Singh,Khashti Ballabh Joshi,Sandeep Verma
标识
DOI:10.1002/cplu.202000464
摘要
Abstract Self‐assembling peptides based on aromatic amino acids can adopt diverse nanostructures which primarily depend on their molecular structures. Therefore, to understand the nature of self‐assembly on the molecular level we rationally designed two constitutional isomers of short aromatic peptides. The first isomer consists of a tyrosine moiety at the N‐terminus and the second isomer consists of a tyrosine moiety at the C‐terminus of the FF peptide, a core recognition motif of Amyloid β peptides. Therefore, it can be considered that both the designed tripeptides are the analogues of the FFF peptide with only atomic(−H) level replacement by −OH functional group on the first and last phenyl ring, respectively. The first isomer self‐assembled into 2D porous nanosheets (“Nanowebs”), however the second isomers produced toroidal shapes with central spheres (“Nano‐Saturn” like assemblies). Interestingly, the presence of the transition‐metal ions (copper, zinc and iron) triggered the self‐assembly of both the peptides into fibrous circular discs, nanomats and nanoplates like assembly.
科研通智能强力驱动
Strongly Powered by AbleSci AI