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Artículo

Biophysical Analysis to Assess the Interaction of CRAC and CARC Motif Peptides of Alpha Hemolysin of Escherichia coli with Membranes

Cané, LucíaIcon ; Guzmán, Fanny; Balatti, Galo EzequielIcon ; Daza Millone, Maria AntonietaIcon ; Pucci Molineris, Melisa ElianaIcon ; Maté, Sabina MaríaIcon ; Martini, María FlorenciaIcon ; Herlax, Vanesa SilvanaIcon
Fecha de publicación: 05/2023
Editorial: American Chemical Society
Revista: Biochemistry
ISSN: 0006-2960
Idioma: Inglés
Tipo de recurso: Artículo publicado
Clasificación temática:
Biofísica

Resumen

Alpha hemolysin of Escherichia coli (HlyA) is a pore-forming protein, which is a prototype of the “Repeat in Toxins” (RTX) family. It was demonstrated that HlyA-cholesterol interaction facilitates the insertion of the toxin into membranes. Putative cholesterol-binding sites, called cholesterol recognition/amino acid consensus (CRAC), and CARC (analogous to CRAC but with the opposite orientation) were identified in the HlyA sequence. In this context, two peptides were synthesized, one derived from a CARC site from the insertion domain of the toxin (residues 341-353) (PEP 1) and the other one from a CRAC site from the domain between the acylated lysines (residues 639-644) (PEP 2), to study their role in the interaction of HlyA with membranes. The interaction of peptides with membranes of different lipid compositions (pure POPC and POPC/Cho of 4:1 and 2:1 molar ratios) was analyzed by surface plasmon resonance and molecular dynamics simulations. Results demonstrate that both peptides interact preferentially with Cho-containing membranes, although PEP 2 presents a lower KD than PEP 1. Molecular dynamics simulation results indicate that the insertion and interaction of PEP 2 with Cho-containing membranes are more prominent than those caused by PEP 1. The hemolytic activity of HlyA in the presence of peptides indicates that PEP 2 was the only one that inhibits HlyA activity, interfering in the binding between the toxin and cholesterol.
Palabras clave: CRAC , CARC , lipid membranes , cholesterol , hemolisina
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info:eu-repo/semantics/openAccess Excepto donde se diga explícitamente, este item se publica bajo la siguiente descripción: Creative Commons Attribution-NonCommercial-ShareAlike 2.5 Unported (CC BY-NC-SA 2.5)
Identificadores
URI: http://hdl.handle.net/11336/220677
URL: https://pubs.acs.org/doi/10.1021/acs.biochem.3c00164
DOI: https://doi.org/10.1021/acs.biochem.3c00164
Colecciones
Articulos(IQUIMEFA)
Articulos de INST.QUIMICA Y METABOLISMO DEL FARMACO (I)
Articulos(SEDE CENTRAL)
Articulos de SEDE CENTRAL
Citación
Cané, Lucía; Guzmán, Fanny; Balatti, Galo Ezequiel; Daza Millone, Maria Antonieta; Pucci Molineris, Melisa Eliana; et al.; Biophysical Analysis to Assess the Interaction of CRAC and CARC Motif Peptides of Alpha Hemolysin of Escherichia coli with Membranes; American Chemical Society; Biochemistry; 62; 12; 5-2023; 1994-2011
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