Venugopalan, Paloth and Kishore, Raghuvansh (2015) Antiparallel Self-Association of a γ,α-Hybrid Peptide: More Relevance of Weak Interactions. Chemistry: an Asian journal. ISSN 1861-471X
Full text not available from this repository. (Request a copy)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 γ,α-hybrid model peptide, Boc-γ-Abz-Gly-OMe. The single-crystal X-ray diffraction analysis revealed the existence of a fully extended β-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-γ-Abz-amide moiety is predominantly preserved in a non-polar environment. The self-association of the energetically more favorable antiparallel β-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 γ-Abz foldamer in appositely designed peptides may encourage unusual β-strand or β-sheet-like self-association and supramolecular organization stabilized via weak attractive forces.
| Item Type: | Article |
|---|---|
| Additional Information: | Copyright of this article belongs to Wiley. |
| Uncontrolled Keywords: | X-ray diffraction; foldamers; peptide design; self-association; weak interactions; β-strand mimics |
| Subjects: | Q Science > QR Microbiology |
| Depositing User: | Dr. K.P.S.Sengar |
| Date Deposited: | 13 Jul 2015 13:04 |
| Last Modified: | 13 Jul 2015 13:04 |
| URI: | http://crdd.osdd.net/open/id/eprint/1632 |
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