Contrasting solution conformations of peptides containing alpha,alpha-dialkylated residues with linear and cyclic side chains

Sudhanand, Prasad and Rao, Balaji R and Balaram, P (1995) Contrasting solution conformations of peptides containing alpha,alpha-dialkylated residues with linear and cyclic side chains. In: Biopolymers, 35 (1). pp. 11-20.

Preview

PDF sudhanand.pdf Download (775kB)

Abstract

The conformational properties of , -dialkylated amino acid residues possessing acyclic (diethylglycine, Deg: di-n-propylglycine, Dpg; di-n-butylglycine, Dbg) and cyclic (1-amino-cycloalkane-1-carboxylic acid, Acnc) side chains have been compared in solution. The five peptides studied by nmr and CD spectroscopy are Boc-Ala-Xxx-Ala-OMe, where Xxx = Deg(I). Dpg (II), Dbg (III), Ac6c (IV), and Ac7c (V). Delineation of solvent-shielded NH groups have been achieved by solvent and temperature dependence of NH chemical shifts in CDCl3 and (CD3)2SO and by paramagnetic radical induced line broadening in pepiide III. In the Dxg peptides the order of solvent exposure of NH groups is Ala(1) > Ala(3) > Dxg(2), whereas in the Acnc peptides the order of solvent exposure of NH groups is Ala(1) > Acnc(2) > Ala(3). The nmr results suggest that Acnc peptides adopt folded -turn conformations with Ala(1) and Acnc(2) occupying i + 1 and i + 2 positions. In contrast, the Dxg peptides favor extended C5 conformations. The conformational differences in the two series are clearly borne out in CD studies. The solution conformations of peptides I-III are distinctly different from the -turn structure observed in crystals. Low temperature nmr spectra recorded immediately after dissolution of crystals of peptide II provide evidence for a structural transition. Introduction of an additional hydrogen-bonding function in Boc-Ala-Dpg-Ala-NHMe (VI) results in a stabilization of a consecutive -turn or incipient 310-helix in solution.

Item Type:	Journal Article
Publication:	Biopolymers
Publisher:	John Wiley & Sons, Inc.
Additional Information:	Copyright of this article belongs to John Wiley & Sons, Inc.
Keywords:	dialkylated;alpha alpha;peptides
Department/Centre:	Division of Biological Sciences > Molecular Biophysics Unit
Date Deposited:	14 Jun 2004
Last Modified:	19 Sep 2010 04:12
URI:	http://eprints.iisc.ac.in/id/eprint/392

Actions (login required)

View Item