Journal
CHEMBIOCHEM
Volume 14, Issue 5, Pages 617-624Publisher
WILEY-V C H VERLAG GMBH
DOI: 10.1002/cbic.201300034
Keywords
antimicrobial peptides; cyclization; drug design; gomesin; native chemical ligation
Funding
- Queensland Smart State Fellowship
- Queensland Government
- Australian Research Council [DP0986281]
- Australian Research Council [DP0986281] Funding Source: Australian Research Council
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Gomesin is an 18-residue peptide originally isolated from the hemocytes of the Brazilian spider Acanthoscurria gomesiana. A broad spectrum of bioactivities have been attributed to gomesin, including in vivo and in vitro cytotoxicity against tumour cells, antimicrobial, antifungal, anti-Leishmania and antimalarial effects. Given the potential therapeutic applications of gomesin, it was of interest to determine if an engineered version with a cyclic backbone has improved stability and bioactivity. Cyclization has been shown to confer enhanced stability and activity to a range of bioactive peptides and, in the case of a cone snail venom peptide, confer oral activity in a pain model. The current study demonstrates that cyclization improves the in vitro stability of gomesin over a 24 hour time period and enhances cytotoxicity against a cancer cell line without being toxic to a noncancerous cell line. In addition, antimalarial activity is enhanced upon cyclization. These findings provide additional insight into the influences of backbone cyclization on the therapeutic potential of peptides.
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