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Conformational and ion binding properties of a cyclic octapeptide, cyclo(Ala‐Leu‐Pro‐Gly) 2
Author(s) -
Jois D. S. Seetharama,
Easwaran K. R. K.,
Bednarek Maria,
Blout E. R.
Publication year - 1992
Publication title -
biopolymers
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.556
H-Index - 125
eISSN - 1097-0282
pISSN - 0006-3525
DOI - 10.1002/bip.360320810
Subject(s) - chemistry , divalent , cyclic peptide , peptide , calcium , acetonitrile , stereochemistry , barium , crystallography , nuclear magnetic resonance spectroscopy , solvent , ion , inorganic chemistry , organic chemistry , biochemistry
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.