Volume 32, Issue 8 pp. 993-1001
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Conformational and ion binding properties of a cyclic octapeptide, cyclo(Ala-Leu-Pro-Gly)2

D. S. Seetharama Jois

D. S. Seetharama Jois

Molecular Biophysics Unit, Indian Institute of Science, Bangalore, India

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K. R. K. Easwaran

K. R. K. Easwaran

Molecular Biophysics Unit, Indian Institute of Science, Bangalore, India

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Maria Bednarek

Maria Bednarek

Department of Biological Chemistry and Molecular Pharmacology, Harvard Medical School, Boston, Massachusetts 02115, USA

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E. R. Blout

E. R. Blout

Department of Biological Chemistry and Molecular Pharmacology, Harvard Medical School, Boston, Massachusetts 02115, USA

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First published: August 1992
Citations: 9

Abstract

The conformation and ion-binding characteristics of a cyclic octapeptide, cyclo(Ala-Leu-Pro-Gly)2, in a liphophilic solvent, acetonitrile, have been studied using CD and nmr spectroscopy. The peptide binds preferentially to divalent cations such as calcium, magnesium, and barium. The conformations of the free cyclic peptide and its calcium complex are very similar with well-defined β- and γ-turns. The cyclic peptide readily forms equimolar and possibly 2 : 1 (peptide:cation) complexes with divalent cations.

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