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Bioactive peptides: Conformational study of a cystinyl cycloheptapeptide in its free and calcium complexed forms
Author(s) -
Zanotti Giancarlo,
Maione Annamaria,
Rossi Filomena,
Saviano Michele,
Pedone Carlo,
Tancredi Teodorico
Publication year - 1993
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.360330710
Subject(s) - chemistry , peptide , stoichiometry , calcium , acetonitrile , hydrogen bond , ring (chemistry) , crystallography , molecular dynamics , ion , stereochemistry , molecule , computational chemistry , organic chemistry , biochemistry
Abstract The disulphide bridged heptapeptidehas been synthesized by classical solution methods. An ion binding study showed the peptide's ability to complex calcium ions with definite stoichiometry. The solution conformation of the peptide in its free and calcium‐complexed form has been investigated by CD and nmr. The model structure derived from nmr data has been energy minimized and the resulting structure investigated by molecular dynamics simulation in water. The structure of the equimolar peptide/Ca 2− complex in acetonitrile at room temperature shows the presence of two transannular hydrogen bonds, with the formation of two ring structures of the C 10 (type VIa) and C 14 type. One peptide unit (Pro‐Pro) is cis , all others are trans. © 1993 John Wiley & Sons, Inc.