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Determination of the disulfide array in sapecin, an antibacterial peptide of Sarcophaga peregrina (flesh fly).

作者信息

Kuzuhara T, Nakajima Y, Matsuyama K, Natori S

机构信息

Faculty of Pharmaceutical Sciences, University of Tokyo.

出版信息

J Biochem. 1990 Apr;107(4):514-8. doi: 10.1093/oxfordjournals.jbchem.a123077.

DOI:10.1093/oxfordjournals.jbchem.a123077
PMID:2358424
Abstract

Sapecin is a 40-residue peptide containing 6 half-cystine residues. The disulfide structure of sapecin was determined by sequencing cystine-containing peptides obtained by digesting sapecin with thermolysin. Results showed that sapecin has a vortical structure fixed by 3 disulfide bonds between cysteine residues 3 and 30, 16 and 36, and 20 and 38, respectively, and that these disulfide bonds are essential for its antibacterial activity.

摘要

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Determination of the disulfide array in sapecin, an antibacterial peptide of Sarcophaga peregrina (flesh fly).
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