iophysical Studies of TOAC Analogs of the Ctx(Ile(21))-Ha Antimicrobial Peptide Using Liposome

Autor(es)

Vicente, Eduardo Festozo ^[1] ; Basso, Luis G. M. ^[2] ; Crusca Junior, Edson ^[3] ; Roque-Borda, Cesar A. ^[4] ; Costa-Filho, Antonio J. ^[5] ; Cilli, Eduardo Maffud ^[6]

Afiliação do(s) autor(es)

^[1] Sao Paulo State Univ, Sch Sci & Engn, Dept Biosyst Engn, UNESP, Rua Domingos Costa Lopes 780, BR-17602496 Tupa, SP - Brazil

^[2] State Univ Northern Rio de Janeiro Darcy Ribeiro, Ctr Sci & Technol, Phys Sci Lab, Ave Alberto Lamego 2000, BR-28013602 Campos Dos Goytacazes, RJ - Brazil

^[3] Sao Paulo State Univ, Inst Biosci Humanities & Exact Sci, Dept Biochem, UNESP, Rua Cristovao Colombo 2265, BR-15054000 Sao Jose Do Rio Preto, SP - Brazil

^[4] Sao Paulo State Univ, Sch Agr & Veterinarian Sci, UNESP, BR-14884900 Jaboticabal, SP - Brazil

^[5] Univ Sao Paulo, Fac Philosophy Sci & Letters Ribeirao Preto, Phys Dept, Ave Bandeirantes 3900, BR-14040901 Ribeirao Preto, SP - Brazil

^[6] Sao Paulo State Univ, Inst Chem, Dept Biochem & Chem Tecnol, UNESP, Rua Prof Francisco Degni 55, BR-14800900 Araraquara, SP - Brazil

• Tipo de documento: Artigo Científico
• Fonte: Brazilian Journal of Physics; v. 52, n. 3 JUN 2022.
• Citações Web of Science: 0

Resumo

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(Ile(21))-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(Ile(21))-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(Ile(21))-Ha and its analogs showed a higher affinity for phosphatidylethanolamine (PE) head groups than sphingomyelin (SM), adopting alpha-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(Ile(21))-Ha peptide modulated by membranes of different lipid compositions and corroborate the barrel-stave model as the mechanism of action of the Ctx(Ile(21))-Ha. (AU)

• Processo FAPESP: 09/10997-7 - Interações com membranas de peptídeos de fusão da glicoproteína s do SARS-CoV
• Beneficiário: Luís Guilherme Mansor Basso
• Modalidade de apoio: Bolsas no Brasil - Doutorado
• Processo FAPESP: 06/01381-4 - Relacao estrutura/funcao de dois peptideos hemoliticos provenientes de uma ra brasileira.
• Beneficiário: Eduardo Maffud Cilli
• Modalidade de apoio: Auxílio à Pesquisa - Regular