A designed β-hairpin peptide

S. K., Awasthi ; S., Raghothama ; Balaram, P. (1995) A designed β-hairpin peptide Biochemical and Biophysical Research Communications, 216 (1). pp. 375-381. ISSN 0006-291X

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Official URL: http://linkinghub.elsevier.com/retrieve/pii/S00062...

Related URL: http://dx.doi.org/10.1006/bbrc.1995.2634


A synthetic octapeptide, Boc-Leu-Val-Val-D-Pro-Gly-Leu-Val-Val-OMe (1) has been designed as a model for a β-hairpin conformation. Circular dichroism spectra in various organic solvents reveal a single negative band at 214-217 nm consistent with β-sheet structures. NMR studies in CDCl3 and C6D6 establish the solvent shielded nature of the Leu(1), Val(3), Leu(6) and Val (8) NH groups. Nuclear Overhauser effects are observed between Val(7) CαH and Val(2) (CαH) protons providing strong support for a beta-hairpin conformation. Several important diagnostic interresidue NOEs establish a Type II′ β-turn conformation for the D-Pro-Gly segment and extended conformations for the amino and carboxyl terminal tripeptide arms. The high solubility of the β-hairpin peptide in organic solvents holds promise for the development of models for three and four stranded β-sheets.

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