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Ion binding of cyclolinopeptide A: An nmr and CD conformational study

✍ Scribed by Teodorico Tancredi; Ettore Benedetti; Maria Grimaldi; Carlo Pedone; Filomena Rossi; Michele Saviano; Piero Andrea Temussi; Giancarlo Zanotti

Publisher
Wiley (John Wiley & Sons)
Year
1991
Tongue
English
Weight
488 KB
Volume
31
Category
Article
ISSN
0006-3525

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✦ Synopsis

SYNOPSIS

CD and nmr techniques have been used to study, in acetonitrile solution, the ion-complexing capability of cyclolinopeptide A (CLA) , a cyclic nonapeptide of sequence cyclo-( Pro-Pro-Phe-Phe-Leu-Ile-Ile-Leu-Val) endowed with remarkable cytoprotective ability in vitro, and the conformation of the Ba2'/ CLA complex.

At room temperature, CLA in acetonitrile shows a proton nmr spectrum characteristic of the coexistence of many different conformers in intermediate exchange. The backbone contains a cis Pro-Pro bond, with all other peptide bonds in the trans conformation.

CLA binds Ba2+ more tightly than the other cations studied, namely K', N a + , Mg2+, and Ca2+; CD data are indicative of the presence of both 1 : 2 (sandwich) and 1 : 1 (equimolar) type complexes, depending on the Ba2+ ion concentration, whereas nmr data are consistent with an equimolar form.

The relevant conformational features of the equimolar Ba2+/CLA complex are that the backbone contains all trans peptide bonds, a type I 6 -P 3 @-turn and a 3 -P 1 y-turn (or a distorted 3 + 9 @-turn). The global shape of the complexed peptide can be described as a bowl, with the concave (polar) side hosting Ba2+ and the convex side predominantly apolar.

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