Venom Peptides Cathelicidin and Lycotoxin Cause Strong Inhibition of Escherichia coli ATP Synthase
Document Type
Article
Publication Date
6-1-2016
Description
Venom peptides are known to have strong antimicrobial activity and anticancer properties. King cobra cathelicidin or OH-CATH (KF-34), banded krait cathelicidin (BF-30), wolf spider lycotoxin I (IL-25), and wolf spider lycotoxin II (KE-27) venom peptides were found to strongly inhibit Escherichia coli membrane bound F1Fo ATP synthase. The potent inhibition of wild-type E. coli in comparison to the partial inhibition of null E. coli by KF-34, BF-30, Il-25, or KE-27 clearly links the bactericidal properties of these venom peptides to the binding and inhibition of ATP synthase along with the possibility of other inhibitory targets. The four venom peptides KF-34, BF-30, IL-25, and KE-27, caused ≥85% inhibition of wild-type membrane bound E.coli ATP synthase. Venom peptide induced inhibition of ATP synthase and the strong abrogation of wild-type E. coli cell growth in the presence of venom peptides demonstrates that ATP synthase is a potent membrane bound molecular target for venom peptides. Furthermore, the process of inhibition was found to be fully reversible.
Citation Information
Azim, Sofiya; McDowell, Derek; Cartagena, Alec; Rodriguez, Ricky; Laughlin, Thomas F.; and Ahmad, Zulfiqar. 2016. Venom Peptides Cathelicidin and Lycotoxin Cause Strong Inhibition of Escherichia coli ATP Synthase. International Journal of Biological Macromolecules. Vol.87 246-251. https://doi.org/10.1016/j.ijbiomac.2016.02.061 PMID: 26930579 ISSN: 0141-8130