Determination of disulfide bridge pattern in ω-conopeptides

Chung, David ; Gaur, Smita ; Bell, John R. ; Ramachandran, J. ; Nadasdi, Laszlo (1995) Determination of disulfide bridge pattern in ω-conopeptides International Journal of Peptide and Protein Research, 46 (3-4). pp. 320-325. ISSN 0367-8377

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Synthetic versions of seven naturally occurring omega-conopeptides were subjected to structural analyses in order to determine their disulfide bridge pattern. The method applied in this study uses a combination of amino-acid composition and peptide sequence analysis of various peptide fragments generated by different enzymatic digestions. A temperature modification in the Edman degradation cycles of a protein sequencer allowed the unambiguous detection of the cleavage of cystine residues. The appearance of the cystine residues in particular cycles of the sequence analysis was characteristic of one or several of the theoretically possible 15 isomers. In the case of multiple choices, possible isomers were further eliminated by the amino-acid and sequence analysis of peptide fragments generated by the enzymatic digestion. All synthetic peptides, SNX-111, -157, -159, -183, -185, -230 and -231, were found to have the same disulfide bridge pattern as determined for the naturally occurring omega-conopeptide G-VI-A, i.e. disulfide bridges between the half-cystines 1-16, 8-20 and 15-25 (using the amino-acid numbering of SNX-111).

Item Type:Article
Source:Copyright of this article belongs to John Wiley and Sons.
Keywords:Conopeptide; Disulfide Bridge Determination; Enzyme Digestion
ID Code:40969
Deposited On:25 May 2011 10:46
Last Modified:25 May 2011 10:46

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