Binding studies of antimicrobial peptides to Escherichia coli cells.
Biochem Biophys Res Commun
; 478(1): 149-153, 2016 09 09.
Article
en En
| MEDLINE
| ID: mdl-27450805
ABSTRACT
Understanding the mechanism of action of antimicrobial peptides is pivotal to the design of new and more active peptides. In the last few years it has become clear that the behavior of antimicrobial peptides on membrane model systems does not always translate to cells; therefore the need to develop methods aimed at capturing details of the interactions of peptides with bacterial cells is compelling. In this work we analyzed binding of two peptides, namely temporin B and TB_KKG6A, to Escherichia coli cells and to Escherichia coli LPS. Temporin B is a natural peptide active against Gram positive bacteria but inactive against Gram negative bacteria, TB_KKG6A is an analogue of temporin B showing activity against both Gram positive and Gram negative bacteria. We found that binding to cells occurs only for the active peptide TB_KKG6A; stoichiometry and affinity constant of this peptide toward Escherichia coli cells were determined.
Palabras clave
Texto completo:
1
Colección:
01-internacional
Base de datos:
MEDLINE
Contexto en salud:
3_ND
Problema de salud:
3_neglected_diseases
/
3_zoonosis
Asunto principal:
Proteínas
/
Membrana Celular
/
Péptidos Catiónicos Antimicrobianos
/
Mapeo de Interacción de Proteínas
/
Escherichia coli
Idioma:
En
Revista:
Biochem Biophys Res Commun
Año:
2016
Tipo del documento:
Article
País de afiliación:
Italia