Effect of C-terminal and N-terminal dimerization and alanine scanning on antibacterial activity of the analogs of the peptide p-BthTX-I

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Autor(es): dc.contributorUniversidade Estadual Paulista (UNESP)-
Autor(es): dc.contributorUniversidade de São Paulo (USP)-
Autor(es): dc.creatorSantos-Filho, Norival Alves-
Autor(es): dc.creatorRighetto, Gabriela Marinho-
Autor(es): dc.creatorPereira, Marina Rodrigues-
Autor(es): dc.creatorPiccoli, Julia Pinto-
Autor(es): dc.creatorAlmeida, Larissa Mathias Teizen-
Autor(es): dc.creatorLeal, Thainá Cristina-
Autor(es): dc.creatorCamargo, Ilana Lopes Baratella Cunha-
Autor(es): dc.creatorCilli, Eduardo Maffud-
Data de aceite: dc.date.accessioned2025-08-21T18:31:48Z-
Data de disponibilização: dc.date.available2025-08-21T18:31:48Z-
Data de envio: dc.date.issued2022-05-01-
Data de envio: dc.date.issued2022-05-01-
Data de envio: dc.date.issued2022-03-01-
Fonte completa do material: dc.identifierhttp://dx.doi.org/10.1002/pep2.24243-
Fonte completa do material: dc.identifierhttp://hdl.handle.net/11449/233532-
Fonte: dc.identifier.urihttp://educapes.capes.gov.br/handle/11449/233532-
Descrição: dc.descriptionThe peptide (p-BthTX-I)2 [(KKYRYHLKPFCKK)2] and its analog des-Lys12,Lys13-(p-BthTX-I)2 [(KKYRYHLKPFC)2] showed activity against bacteria and potential specificity against prokaryotic cells. In this study, we synthesized the peptide des-Cys11,Lys12,Lys13-(p-BthTX-I)2K [(KKYRYHLKPF)2K] with a Lys instead of a Cys residue in the dimerization step, beginning the SPPS with Fmoc-Lys(Fmoc)-OH. This change avoided Cys oxidation, decreasing one step in the original peptide synthesis and obtaining a smaller and more stable peptide. The antimicrobial activity of the peptide des-Cys11,Lys12,Lys13-(p-BthTX-I)2K was superior to that of the (p-BthTX-I)2 peptide against the bacterial strains tested. Additionally, to evaluate the impact of the linker position on peptide dimerization, we synthesized peptide E(p-BthTX-I)2 [E(KKYRYHLKPFCKK)2] using Fmoc-Glu-OH at the end of the synthesis. This N-terminal dimeric peptide did not increase the antibacterial activity, indicating that the free N-terminal is essential for (p-BthTX-I)2 activity. Additionally, we observed lower antimicrobial activity by substituting positive and aromatic residues with Ala in the alanine scanning assay, irrespective of the amino acid change, indicating that each amino acid is essential for the mechanism of action of the peptide. Therefore, we demonstrated that the (p-BthTX-I)2 analog, which is shorter and synthesized by an easier process leading to a more stable peptide, is the most antibacterial active peptide against multidrug-resistant bacteria and does not increase hemolysis activity.-
Descrição: dc.descriptionConselho Nacional de Desenvolvimento Científico e Tecnológico (CNPq)-
Descrição: dc.descriptionFundação de Amparo à Pesquisa do Estado de São Paulo (FAPESP)-
Descrição: dc.descriptionInstituto de Química UNESP-
Descrição: dc.descriptionInstituto de Física de São Carlos USP, São Carlos-
Descrição: dc.descriptionInstituto de Química UNESP-
Descrição: dc.descriptionFAPESP: 2012/15346-7-
Descrição: dc.descriptionFAPESP: 2013/07600-3-
Descrição: dc.descriptionFAPESP: 2014/05538-1-
Idioma: dc.languageen-
Relação: dc.relationPeptide Science-
???dc.source???: dc.sourceScopus-
Palavras-chave: dc.subject(p-BthTX-I)2-
Palavras-chave: dc.subjectAla scan-
Palavras-chave: dc.subjectantimicrobial peptides-
Palavras-chave: dc.subjectmultidrug-resistant bacteria-
Palavras-chave: dc.subjectp-BthTX-I-
Título: dc.titleEffect of C-terminal and N-terminal dimerization and alanine scanning on antibacterial activity of the analogs of the peptide p-BthTX-I-
Tipo de arquivo: dc.typelivro digital-
Aparece nas coleções:Repositório Institucional - Unesp

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