Conformations of dehydrophenylalanine containing peptides: NMR studies on three tripeptides with a central dehydrophenylalanyl residue

Chauhan, V. S. ; Sharma, Ashwani K. ; Uma, K. ; Paul, P. K. C. ; Balaram, P. (1987) Conformations of dehydrophenylalanine containing peptides: NMR studies on three tripeptides with a central dehydrophenylalanyl residue International journal of peptide and protein research, 29 (1). pp. 126-133. ISSN 0367-8377

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Official URL: http://onlinelibrary.wiley.com/doi/10.1111/j.1399-...

Related URL: http://dx.doi.org/10.1111/j.1399-3011.1989.tb00194.x

Abstract

Three tripeptides containing a central Z-dehydrophenylalanine residue (Δz-Phe), Boc-L-Phe-Δz-Phe-X-OMe (X = L-Val 1, L-Leu 2 and X = L-Ala 3) have been synthesized and their solution conformations investigated by 270 MHz 1H NMR spectroscopy. In all three peptides, conformations involving the X residue NH in an intramolecular hydrogen bond were favoured in CDCl3 solutions. Studies of the nuclear Overhauser effect (NOE) provided support for a Type II β turn conformation in these peptides with Phe and Δz-Phe occupying the i + 1 and i + 2 positions, respectively. Significantly different conformations lacking any intramolecular hydrogen bonds were observed for peptide 1 in (CD3)2SO. NOE results were consistent with a significant population of molecules having semi-extended conformations (∅ > 100°) at the Δz-Phe residue.

Item Type:Article
Source:Copyright of this article belongs to Munksgaard International Publishers.
Keywords:Dehydrophenylalanine Peptides; β Turns; Nuclear Overhauser Effects
ID Code:8224
Deposited On:26 Oct 2010 12:09
Last Modified:16 May 2016 18:16

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