%A Paloth Venugopalan
%A Raghuvansh Kishore
%O Copyright of this article belongs to Wiley.
%J Chemistry: an Asian journal
%T Antiparallel Self-Association of a ?,?-Hybrid Peptide: More Relevance of Weak Interactions.
%X To learn how a preorganized peptide-based molecular template, together with diverse weak non-covalent interactions, leads to an effective self-association, we investigated the conformational characteristics of a simple ?,?-hybrid model peptide, Boc-?-Abz-Gly-OMe. The single-crystal X-ray diffraction analysis revealed the existence of a fully extended ?-strand-like structure stabilized by two non-conventional C-H???O=C intramolecular H-bonds. The 2D (1) H?NMR ROESY experiment led us to propose that the flat topology of the urethane-?-Abz-amide moiety is predominantly preserved in a non-polar environment. The self-association of the energetically more favorable antiparallel ?-strand-mimic in solid-state engenders an unusual 'flight of stairs' fabricated through face-to-face and edge-to-edge Ar???Ar interactions. In conjunction with FT-IR spectroscopic analysis in chloroform, we highlight that conformationally semi-rigid ?-Abz foldamer in appositely designed peptides may encourage unusual ?-strand or ?-sheet-like self-association and supramolecular organization stabilized via weak attractive forces.
%K X-ray diffraction; foldamers; peptide design; self-association; weak interactions; ?-strand mimics
%D 2015
%I Wiley
%L open1632