Conformational restrictions of peptides via backbone modification: solution and crystal-state analysis of Boc-L-Pro-ΔZPhe-Gly-NH2

Piazzesi, Anna Maria ; Bardi, Renaato ; Crisma, Marco ; Banora, Gian Maria ; Toniolo, Claudio ; Chauhan, Virander Singh ; Kaur, Paramjeet ; Uma, Kuchibhotla ; Balaram, Padmanabhan (1991) Conformational restrictions of peptides via backbone modification: solution and crystal-state analysis of Boc-L-Pro-ΔZPhe-Gly-NH2 Gazzetta Chimica Italiana, 121 . pp. 1-7. ISSN 0016-5603

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Abstract

An Nα-protected model tripeptide amide containing, in the central position, an α,β-dehydrophenylalanine (Z-configurational isomer), Boc-L-Pro-ΔZ-Phe-Gly-NH2 (Boc, tert-butyloxycarbonyl), has been synthesized by solution methods and fully characterized. IR absorption and 1H NMR studies provided evidence for the occurrence of a significant population of a conformer containing two consecutive, intramolecularly H-bonded (type II-III') β-bends in solution. However, an X-ray diffraction analysis clearly indicates that only the type-II β-bend structure survives in the crystal state.

Item Type:Article
Source:Copyright of this article belongs to Società Chimica Italiana, Roma.
ID Code:77512
Deposited On:12 Jan 2012 14:37
Last Modified:18 May 2016 20:45

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