Effects of Dimerization, Dendrimerization, and Chirality in p-BthTX-I Peptide Analogs on the Antibacterial Activity and Enzymatic Inhibition of the SARS-CoV-2 PLpro Protein

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Autor(es): dc.contributorUniversidade Estadual Paulista (UNESP)-
Autor(es): dc.contributorUniversidade de São Paulo (USP)-
Autor(es): dc.creatorBitencourt, Natália Vitória-
Autor(es): dc.creatorRighetto, Gabriela Marinho-
Autor(es): dc.creatorCamargo, Ilana Lopes Baratella Cunha-
Autor(es): dc.creatorde Godoy, Mariana Ortiz-
Autor(es): dc.creatorGuido, Rafael Victorio Carvalho-
Autor(es): dc.creatorOliva, Glaucius-
Autor(es): dc.creatorSantos-Filho, Norival Alves-
Autor(es): dc.creatorCilli, Eduardo Maffud-
Data de aceite: dc.date.accessioned2025-08-21T17:53:43Z-
Data de disponibilização: dc.date.available2025-08-21T17:53:43Z-
Data de envio: dc.date.issued2023-07-29-
Data de envio: dc.date.issued2023-07-29-
Data de envio: dc.date.issued2023-01-31-
Fonte completa do material: dc.identifierhttp://dx.doi.org/10.3390/pharmaceutics15020436-
Fonte completa do material: dc.identifierhttp://hdl.handle.net/11449/248440-
Fonte: dc.identifier.urihttp://educapes.capes.gov.br/handle/11449/248440-
Descrição: dc.descriptionRecent studies have shown that the peptide [des-Cys11,Lys12,Lys13-(p-BthTX-I)2K] (p-Bth) is a p-BthTX-I analog that shows enhanced antimicrobial activity, stability and hemolytic activity, and is easy to obtain compared to the wild-type sequence. This molecule also inhibits SARS-CoV-2 viral infection in Vero cells, acting on SARS-CoV-2 PLpro enzymatic activity. Thus, the present study aimed to assess the effects of structural modifications to p-Bth, such as dimerization, dendrimerization and chirality, on the antibacterial activity and inhibitory properties of PLpro. The results showed that the dimerization or dendrimerization of p-Bth was essential for antibacterial activity, as the monomeric structure led to a total loss of, or significant reduction in, bacterial activities. The dimers and tetramers obtained using branched lysine proved to be prominent compounds with antibacterial activity against Gram-positive and Gram-negative bacteria. In addition, hemolysis rates were below 10% at the corresponding concentrations. Conversely, the inhibitory activity of the PLpro of SARS-CoV-2 was similar in the monomeric, dimeric and tetrameric forms of p-Bth. Our findings indicate the importance of the dimerization and dendrimerization of this important class of antimicrobial peptides, which shows great potential for antimicrobial and antiviral drug-discovery campaigns.-
Descrição: dc.descriptionCoordenação de Aperfeiçoamento de Pessoal de Nível Superior (CAPES)-
Descrição: dc.descriptionDepartment of Biochemistry and Organic Chemistry Institute of Chemistry São Paulo State University (UNESP), SP-
Descrição: dc.descriptionSão Carlos Institute of Physics University of São Paulo, SP-
Descrição: dc.descriptionDepartment of Biochemistry and Organic Chemistry Institute of Chemistry São Paulo State University (UNESP), SP-
Idioma: dc.languageen-
Relação: dc.relationPharmaceutics-
???dc.source???: dc.sourceScopus-
Palavras-chave: dc.subjectantimicrobial peptide-
Palavras-chave: dc.subjectCOVID-19-
Palavras-chave: dc.subjectdendrimers-
Palavras-chave: dc.subjectmultidrug-resistant bacteria-
Palavras-chave: dc.subjectp-Bth-
Palavras-chave: dc.subjectp-BthTX-I-
Palavras-chave: dc.subjectPLpro-
Palavras-chave: dc.subjectSARS-CoV-2-
Título: dc.titleEffects of Dimerization, Dendrimerization, and Chirality in p-BthTX-I Peptide Analogs on the Antibacterial Activity and Enzymatic Inhibition of the SARS-CoV-2 PLpro Protein-
Tipo de arquivo: dc.typelivro digital-
Aparece nas coleções:Repositório Institucional - Unesp

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