Conformationally restricted peptides: solution conformation of tetra and hepta peptides containing α,β-dehydrophenylalanine residues in alternate positions

Chauhan, Virander Singh ; Jain, Ratanmani ; Singh, Mahak (1994) Conformationally restricted peptides: solution conformation of tetra and hepta peptides containing α,β-dehydrophenylalanine residues in alternate positions Tetrahedron, 50 (3). pp. 907-920. ISSN 0040-4020

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Official URL: http://linkinghub.elsevier.com/retrieve/pii/S00404...

Related URL: http://dx.doi.org/10.1016/S0040-4020(01)80805-X

Abstract

Two model peptides containing dehydrophenylalanine, a tetrapeptide 1 (Ac- ΔzPhe-Pro-ΔzPhe-Ala-OMe) and a heptapeptide 2 (Boc-Gly-ΔzPhe-Val-ΔzPhe-Ala-ΔzPhe-Leu-OMe) have been synthesised and their solution conformations investigated by NMR and circular dichroism techniques. Assignment of amide protons and their involvement in intramolecular hydrogen bonding have been made by solvent and temperature dependence studies. These conformation studies indicate the presence of an incipient 310-helix in tetrapeptide 1, with two consecutive β-turns and a right handed 310-helix in heptapeptide 2. The results establish the potential of ΔzPhe residues to favour 310-helical conformations with δzPhe occupying alternate positions in the peptide. A comparison of solution conformation of analogous peptides containing Aib residue in place of ΔzPhe is also presented. These residues appear to induce similar conformation constraints in small peptides.

Item Type:Article
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ID Code:8274
Deposited On:26 Oct 2010 11:53
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