BIOACTIVE PEPTIDES - CONFORMATIONAL STUDY OF A CYSTINYL CYCLOHEPTAPEPTIDE IN ITS FREE AND CALCIUM COMPLEXED FORMS(621 views) Zanotti G, Maione A, Rossi F, Saviano M, Pedone C, Tancredi T
Affiliations: Istituto Chimica MIB del CNR, Via Toiano 6, 80072 Arco Felice, Napoli, Italy
References: Not available.
BIOACTIVE PEPTIDES - CONFORMATIONAL STUDY OF A CYSTINYL CYCLOHEPTAPEPTIDE IN ITS FREE AND CALCIUM COMPLEXED FORMS
The disulphide bridged heptapeptide [GRAPHICS] has 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/Ca2+ 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.
BIOACTIVE PEPTIDES - CONFORMATIONAL STUDY OF A CYSTINYL CYCLOHEPTAPEPTIDE IN ITS FREE AND CALCIUM COMPLEXED FORMS
Kállay C, Dávid A, Timári S, Nagy EM, Sanna D, Garribba E, Micera G, De Bona P, Pappalardo G, Rizzarelli E, Sóvágó I * Copper(II) complexes of rat amylin fragments(466 views) Dalton T (ISSN: 1477-9234, 1477-9226, 1477-9234electronic), 2011 Oct 14; 40(38): 9711-9721. Impact Factor:3.838 ViewExport to BibTeXExport to EndNote