Determination of the Disulfide Array in Sapecin, an Antibacterial Peptide of Sarcophaga Peregrina (flesh Fly)

Overview

Journal J Biochem

Publisher Oxford University Press

Specialty Biochemistry

Date 1990 Apr 1

PMID 2358424

Citations 10

Authors

T Kuzuhara

Y Nakajima

K Matsuyama

S Natori

Affiliations

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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.

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