Biophysical Studies of TOAC Analogs of the Ctx(Ile21)-Ha Antimicrobial Peptide Using Liposomes

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Autor(es): dc.contributorUniversidade Estadual Paulista (UNESP)-
Autor(es): dc.contributor2000-
Autor(es): dc.contributorUniversidade de São Paulo (USP)-
Autor(es): dc.creatorVicente, Eduardo Festozo-
Autor(es): dc.creatorBasso, Luis G. M.-
Autor(es): dc.creatorCrusca Junior, Edson-
Autor(es): dc.creatorRoque-Borda, Cesar A.-
Autor(es): dc.creatorCosta-Filho, Antonio J.-
Autor(es): dc.creatorCilli, Eduardo Maffud-
Data de aceite: dc.date.accessioned2025-08-21T20:03:08Z-
Data de disponibilização: dc.date.available2025-08-21T20:03:08Z-
Data de envio: dc.date.issued2022-04-29-
Data de envio: dc.date.issued2022-04-29-
Data de envio: dc.date.issued2022-06-01-
Fonte completa do material: dc.identifierhttp://dx.doi.org/10.1007/s13538-022-01077-9-
Fonte completa do material: dc.identifierhttp://hdl.handle.net/11449/230540-
Fonte: dc.identifier.urihttp://educapes.capes.gov.br/handle/11449/230540-
Descrição: dc.descriptionAntimicrobial 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.-
Descrição: dc.descriptionDepartment of Biosystem Engineering School of Sciences and Engineering São Paulo State University (Unesp), Rua Domingos da Costa Lopes, 780-
Descrição: dc.descriptionPhysical Sciences Laboratory Center of Science and Technology State University of Northern Rio de Janeiro Darcy Ribeiro Avenida Alberto Lamego 2000, RJ-
Descrição: dc.descriptionDepartment of Biochemistry Institute of Biosciences Humanities and Exact Sciences São Paulo State University (Unesp), Rua Cristóvão Colombo, 2265-
Descrição: dc.descriptionSchool of Agricultural and Veterinarian Sciences São Paulo State University (Unesp)-
Descrição: dc.descriptionPhysics Department Faculty of Philosophy Sciences and Letters at Ribeirão Preto University of Sao Paulo, Avenida Bandeirantes, 3900, São Paulo-
Descrição: dc.descriptionDepartment of Biochemistry and Chemistry Tecnology Institute of Chemistry São Paulo State University (Unesp), Rua Prof. Francisco Degni, 55, São Paulo-
Descrição: dc.descriptionDepartment of Biosystem Engineering School of Sciences and Engineering São Paulo State University (Unesp), Rua Domingos da Costa Lopes, 780-
Descrição: dc.descriptionDepartment of Biochemistry Institute of Biosciences Humanities and Exact Sciences São Paulo State University (Unesp), Rua Cristóvão Colombo, 2265-
Descrição: dc.descriptionSchool of Agricultural and Veterinarian Sciences São Paulo State University (Unesp)-
Descrição: dc.descriptionDepartment of Biochemistry and Chemistry Tecnology Institute of Chemistry São Paulo State University (Unesp), Rua Prof. Francisco Degni, 55, São Paulo-
Idioma: dc.languageen-
Relação: dc.relationBrazilian Journal of Physics-
???dc.source???: dc.sourceScopus-
Palavras-chave: dc.subjectAntimicrobial peptide-
Palavras-chave: dc.subjectCD-
Palavras-chave: dc.subjectEPR-
Palavras-chave: dc.subjectFluorescence-
Palavras-chave: dc.subjectPeptide membrane interaction-
Palavras-chave: dc.subjectPhospholipid head group-
Título: dc.titleBiophysical Studies of TOAC Analogs of the Ctx(Ile21)-Ha Antimicrobial Peptide Using Liposomes-
Tipo de arquivo: dc.typelivro digital-
Aparece nas coleções:Repositório Institucional - Unesp

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