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J Pept Sci. 1995 May-Jun;1(3):207-15.

Determination of disulphide bridges in PG-2, an antimicrobial peptide from porcine leukocytes.

Author information

1
Department of Medicine, University of California, Los Angeles 90095, USA.

Abstract

We determined the cysteine connectivity of protegrin PG-2, a leukocyte-derived antimicrobial peptide, by performing sequential enzyme digestions with chymotrypsin and thermolysin, and monitoring each digest by direct liquid chromatography-electrospray mass spectrometric analysis. This approach resolved the disulphide pairing pattern unambiguously with only picomolar amounts of PG-2. The inferred cysteine connectivity was confirmed by traditional amino acid composition analyses using nanomolar amounts of the protegrin. The results suggest that protegrins will assume a tachyplesin-like, disulphide-stabilized anti-parallel beta-sheet configuration in solution.

PMID:
9222998
DOI:
10.1002/psc.310010308
[Indexed for MEDLINE]

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