Antiparallel Self-Association of a γ,α-Hybrid Peptide: More Relevance of Weak Interactions.
IR@IMTECH: CSIR-Institute of Microbial Technology, Chandigarh
View Archive Info| Field | Value | |
| Title |
Antiparallel Self-Association of a γ,α-Hybrid Peptide: More Relevance of Weak Interactions.
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| Creator |
Venugopalan, Paloth
Kishore, Raghuvansh |
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| Subject |
QR Microbiology
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| Description |
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.
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| Publisher |
Wiley
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| Date |
2015-05-12
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| Type |
Article
PeerReviewed |
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| Relation |
http://onlinelibrary.wiley.com/doi/10.1002/asia.201500373/pdf
http://crdd.osdd.net/open/1632/ |
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| Identifier |
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
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