Generic placeholder image

Protein & Peptide Letters


ISSN (Print): 0929-8665
ISSN (Online): 1875-5305

Cm38: A New Antimicrobial Peptide Active Against Klebsiella pneumoniae is Homologous to Cn11

Author(s): Duenas-Cuellar, R.A., Kushmerick, C., Naves, L.A., Batista, I.F.C., Guerrero-Vargas, J.A., Pires Jr., O.R., Wagner Fontes and Mariana S. Castro

Volume 22 , Issue 2 , 2015

Page: [164 - 172] Pages: 9

DOI: 10.2174/092986652202150128143048

Price: $65


Antimicrobial peptides (AMPs) represent a large and ubiquitous group of peptides. The current crisis in antibiotic therapy has led to an intensified search for new antimicrobial agents. In this regard, scorpion venom constitutes a rich source of biologically active peptides including AMPs. In the present study, the purification of a novel peptide with antimicrobial activity against the Gram-negative bacteria Klebsiella pneumoniae is described. This antimicrobial peptide, named Cm38, was purified from Centruroides margaritatus scorpion venom using a two-step chromatographic strategy using C8 and C18 columns. This toxin inhibits the proliferation of the Gram-negative bacteria Klebsiella pneumoniae with a Minimal Inhibitory Concentration (MIC) of 64 μM. An analysis of the N-terminal sequence of Cm38 revealed a close structural relationship to Cn11, a Na+-channel modulator toxin previously isolated from Centruroides noxius scorpion venom. Therefore, to test Cm38 for effects on ion channels, we measured its effects on action potential firing in cultured dorsal root ganglion neurons. Cm38 depolarized and increased action potential firing in a subset of neurons tested. The present work reports a new peptide related to Cn11 with antimicrobial properties that is also active in neurons.

Keywords: Action potential firing, antimicrobial peptide, Centruroides margaritatus, Cn11, scorpion.

Graphical Abstract

Rights & Permissions Print Export Cite as
© 2022 Bentham Science Publishers | Privacy Policy