Structure and function study of peptides derived from E. coli alpha hemolysin for the construction of an immunotoxin

FANNY GUZMÁN; HERLAX VANESA; LUCÍA CANÉ; SABINA MATÉ

Congreso; Reunión Conjunta de Sociedades de BioCiencias; 2017

Escherichia coli alpha hemolysin (HlyA) is a pore-forming protein which belongs to the family of 'Repeat in toxins'(RTX). On the basis of experimental data and structural predictions, four peptides derived from HlyA were synthesized: PEP 1: transmembrane domain described as hemolytically active.PEP 2: also a transmembrane domain which sequence corresponds to a cholesterol binding domain (CARC).PEP 3: similar to PEP2 but with residue Y347 substituted by A.PEP 4: similar to PEP2 but with a CRAC sequence (?cholesterol recognition/interaction amino acid consensus domain?). The aims of this work were to find an hemolytic peptide for the construction of an immunotoxin, and to evaluate the role of Y347 in the interaction with membrane.