877117-68-5Relevant academic research and scientific papers
Formation of toroids by self-assembly of an α-α Corner mimetic: Supramolecular cyclization
Podder, Debasish,Bera, Santu,Debnath, Mintu,Das, Tanmay,Haldar, Debasish
, p. 7583 - 7590 (2017/09/27)
An α-α corner mimetic self-assembles to form a rod-like supramolecular structure which bends and closes end-to-end like a cyclization reaction to form uniform toroids. Each peptide fragment containing l-leucine, α-aminoisobutyric acid (Aib) and l-tyrosine forms rigid 310 helical structures stabilized by multiple intramolecular N-H?O hydrogen bonds. Two 310 helices are connected by the spacer 3-aminomethyl-benzylamine and maintain an angular distance of 120° and therefore mimic the α-α corner motif of a protein super secondary structure. The individual α-α corner subunits are themselves regularly interlinked through multiple water mediated intermolecular hydrogen-bonding interactions to form the rod-like supramolecular structure and toroids. The formation of the supramolecular structure has been proven with X-ray crystallography and other spectroscopic techniques. The cyclization of the supramolecular structure and toroid formation were studied by optical microscope, AFM and FE-SEM experiments. Despite other assignments such as exfoliation of graphene from graphite, the compound exhibits significant memory to finally produce the toroids.
