@article{open1632,
           month = {May},
           title = {Antiparallel Self-Association of a {\ensuremath{\gamma}},{\ensuremath{\alpha}}-Hybrid Peptide: More Relevance of Weak Interactions.},
          author = {Paloth Venugopalan and Raghuvansh Kishore},
       publisher = {Wiley},
            year = {2015},
            note = {Copyright of this article belongs to Wiley.},
         journal = {Chemistry: an Asian journal},
        keywords = {X-ray diffraction; foldamers; peptide design; self-association; weak interactions; {\ensuremath{\beta}}-strand mimics},
             url = {http://crdd.osdd.net/open/1632/},
        abstract = {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 {\ensuremath{\gamma}},{\ensuremath{\alpha}}-hybrid model peptide, Boc-{\ensuremath{\gamma}}-Abz-Gly-OMe. The single-crystal X-ray diffraction analysis revealed the existence of a fully extended {\ensuremath{\beta}}-strand-like structure stabilized by two non-conventional C-H{$\cdot$}{$\cdot$}{$\cdot$}O=C intramolecular H-bonds. The 2D (1) H NMR ROESY experiment led us to propose that the flat topology of the urethane-{\ensuremath{\gamma}}-Abz-amide moiety is predominantly preserved in a non-polar environment. The self-association of the energetically more favorable antiparallel {\ensuremath{\beta}}-strand-mimic in solid-state engenders an unusual 'flight of stairs' fabricated through face-to-face and edge-to-edge Ar{$\cdot$}{$\cdot$}{$\cdot$}Ar interactions. In conjunction with FT-IR spectroscopic analysis in chloroform, we highlight that conformationally semi-rigid {\ensuremath{\gamma}}-Abz foldamer in appositely designed peptides may encourage unusual {\ensuremath{\beta}}-strand or {\ensuremath{\beta}}-sheet-like self-association and supramolecular organization stabilized via weak attractive forces.}
}