Involvement of cysteine residues in the biological activity of the active fragments of guinea pig neutrophil cationic peptides.

Infection and Immunity
S YomogidaT Yamashita

Abstract

Guinea pig neutrophil cationic peptides (GNCPs) are single-chain polypeptides with 31 amino acid residues containing six cysteine residues, which exhibit both antibacterial and histamine-releasing activities in vitro. In this study, the role of the sulfhydryl groups in defining the antibacterial and histamine-releasing activities of the active fragments of GNCP-1 (Arg-1 to Tyr-14 [Arg-1-Tyr-14] and Arg-15-Tyr-27 peptides) was examined by using peptides containing alkylated or nonalkylated sulfhydryl groups. Alkylation slightly increased the histamine-releasing activity of the Arg-15-Tyr-27 (RRLGTCIFQNRVY) peptide but abrogated the antibacterial activity. Alkylation of the Arg-1-Tyr-14 (RRCICTTRTCRFPY) peptide similarly reduced the antibacterial activity of this fragment but had minimal effect on the histamine-releasing activity. These findings suggest that cysteine residues with free sulfhydryl groups play an important role in the expression of the antibacterial activity of the active fragments of GNCP-1.

References

May 22, 1992·Biochimica Et Biophysica Acta·W BellamyM Tomita
Nov 1, 1990·The Journal of Clinical Investigation·J K Spitznagel
Jul 15, 1988·Annals of Internal Medicine·R I LehrerJ T Curnutte
Dec 8, 1993·Biochimica Et Biophysica Acta·Y HashimotoT Yamashita

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Citations

Jan 1, 1997·Comparative Biochemistry and Physiology. Part B, Biochemistry & Molecular Biology·S YomogidaT Yamashita

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