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Molecules. 2018 Jul 16;23(7). pii: E1733. doi: 10.3390/molecules23071733.

The Biological and Biophysical Properties of the Spider Peptide Gomesin.

Author information

1
School of Pharmacy and Biomedical Sciences, Curtin Health Innovation Research Institute and Curtin Institute for Computation, Curtin University, GPO Box U1987, Perth WA 6845, Australia. john.d.tanner@student.curtin.edu.au.
2
School of Pharmacy and Biomedical Sciences, Curtin Health Innovation Research Institute and Curtin Institute for Computation, Curtin University, GPO Box U1987, Perth WA 6845, Australia. evelyne.deplazes@curtin.edu.au.
3
School of Pharmacy and Biomedical Sciences, Curtin Health Innovation Research Institute and Curtin Institute for Computation, Curtin University, GPO Box U1987, Perth WA 6845, Australia. r.mancera@curtin.edu.au.

Abstract

This review summarises the current knowledge of Gomesin (Gm), an 18-residue long, cationic anti-microbial peptide originally isolated from the haemocytes of the Brazilian tarantula Acanthoscurria gomesiana. The peptide shows potent cytotoxic activity against clinically relevant microbes including Gram-positive and Gram-negative bacteria, fungi, and parasites. In addition, Gm shows in-vitro and in-vivo anti-cancer activities against several human and murine cancers. The peptide exerts its cytotoxic activity by permeabilising cell membranes, but the underlying molecular mechanism of action is still unclear. Due to its potential as a therapeutic agent, the structure and membrane-binding properties, as well as the leakage and cytotoxic activities of Gm have been studied using a range of techniques. This review provides a summary of these studies, with a particular focus on biophysical characterisation studies of peptide variants that have attempted to establish a structure-activity relationship. Future studies are still needed to rationalise the binding affinity and cell-type-specific selectivity of Gm and its variants, while more pre-clinical studies are required to develop Gm into a therapeutically useful peptide.

KEYWORDS:

anti-cancer peptides; anti-microbial peptides; peptide-membrane interactions; peptides; rational drug design; spider peptides; structure-activity relationship; toxins

PMID:
30012962
PMCID:
PMC6099743
DOI:
10.3390/molecules23071733
[Indexed for MEDLINE]
Free PMC Article

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