Author(s): Vicente, Eduardo Festozo [UNESP] ; Basso, Luis G. M. ; Crusca Junior, Edson [UNESP] ; Roque-Borda, Cesar A. [UNESP] ; Costa-Filho, Antonio J. ; Cilli, Eduardo Maffud [UNESP]
Date: 2022
Persistent ID: http://hdl.handle.net/11449/230540
Origin: Oasisbr
Subject(s): Antimicrobial peptide; CD; EPR; Fluorescence; Peptide membrane interaction; Phospholipid head group
Made available in DSpace on 2022-04-29T08:40:42Z (GMT). No. of bitstreams: 0 Previous issue date: 2022-06-01
Antimicrobial peptides (AMP) are innate components of the defense system of many forms of life, composing the first line of defense from invading pathogens. Among many AMPs described in several databases, the Ctx(Ile21)-Ha antimicrobial peptide has been proven as a very promising molecule for applications in different areas. Nonetheless, there is still a lack of information about the interactions between the peptide and the different lipid components of the membrane. In this way, this study presents a biophysical approach using circular dichroism, fluorescence, and electron spin resonance (ESR) to analyze how the interactions of the Ctx(Ile21)-Ha antimicrobial peptide and its TOAC-labeled analogs with specific phospholipid head groups can modulate structure, peptide dynamics, and membrane integrity. As a result, Ctx(Ile21)-Ha and its analogs showed a higher affinity for phosphatidylethanolamine (PE) head groups than sphingomyelin (SM), adopting α-helical coiled-coil structures in PE membranes, but not in SM membranes. ESR data indicated that all peptides bind to the liposomes to different extents. The present results help to understand the conformational and dynamical changes of the Ctx(Ile21)-Ha peptide modulated by membranes of different lipid compositions and corroborate the barrel-stave model as the mechanism of action of the Ctx(Ile21)-Ha.
Department of Biosystem Engineering School of Sciences and Engineering São Paulo State University (Unesp), Rua Domingos da Costa Lopes, 780
Physical Sciences Laboratory Center of Science and Technology State University of Northern Rio de Janeiro Darcy Ribeiro Avenida Alberto Lamego 2000, RJ
Department of Biochemistry Institute of Biosciences Humanities and Exact Sciences São Paulo State University (Unesp), Rua Cristóvão Colombo, 2265
School of Agricultural and Veterinarian Sciences São Paulo State University (Unesp)
Physics Department Faculty of Philosophy Sciences and Letters at Ribeirão Preto University of Sao Paulo, Avenida Bandeirantes, 3900, São Paulo
Department of Biochemistry and Chemistry Tecnology Institute of Chemistry São Paulo State University (Unesp), Rua Prof. Francisco Degni, 55, São Paulo
Department of Biosystem Engineering School of Sciences and Engineering São Paulo State University (Unesp), Rua Domingos da Costa Lopes, 780
Department of Biochemistry Institute of Biosciences Humanities and Exact Sciences São Paulo State University (Unesp), Rua Cristóvão Colombo, 2265
School of Agricultural and Veterinarian Sciences São Paulo State University (Unesp)
Department of Biochemistry and Chemistry Tecnology Institute of Chemistry São Paulo State University (Unesp), Rua Prof. Francisco Degni, 55, São Paulo
