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 (2023)
- Authors:
- Bitencourt, Natália Vitória - Universidade Estadual Paulista Júlio de Mesquita Filho (UNESP)
- Righetto, Gabriela Marinho
- Camargo, Ilana Lopes Baratella da Cunha
- Godoy, Mariana Ortiz de
- Guido, Rafael Victorio Carvalho
- Oliva, Glaucius
- Santos Filho, Norival Alves - Universidade Estadual Paulista Júlio de Mesquita Filho (UNESP)
- Cilli, Eduardo Maffud - Universidade Estadual Paulista Júlio de Mesquita Filho (UNESP)
- USP affiliated authors: CAMARGO, ILANA LOPES BARATELLA DA CUNHA - IFSC ; GUIDO, RAFAEL VICTÓRIO CARVALHO - IFSC ; OLIVA, GLAUCIUS - IFSC ; RIGHETTO, GABRIELA MARINHO - IFSC ; GODOY, MARIANA ORTIZ DE - IFSC
- Unidade: IFSC
- DOI: 10.3390/pharmaceutics15020436
- Subjects: COVID-19; CORONAVIRUS; PEPTÍDEOS; RESISTÊNCIA MICROBIANA ÀS DROGAS
- Keywords: p-BthTX-I; Multidrug-resistant bacteria; Antimicrobial peptide; Dendrimers; PLpro; SARS-CoV-2; COVID-19
- Agências de fomento:
- Language: Inglês
- Imprenta:
- Source:
- Título do periódico: Pharmaceutics
- ISSN: 1999-4923
- Volume/Número/Paginação/Ano: v. 15, n. 2, p. 436-1-436-17 + supplementary materials: 1-8, Feb. 2023
- Este periódico é de acesso aberto
- Este artigo é de acesso aberto
- URL de acesso aberto
- Cor do Acesso Aberto: gold
- Licença: cc-by
-
ABNT
BITENCOURT, Natália Vitória et al. 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. Pharmaceutics, v. 15, n. 2, p. 436-1-436-17 + supplementary materials: 1-8, 2023Tradução . . Disponível em: https://doi.org/10.3390/pharmaceutics15020436. Acesso em: 28 abr. 2024. -
APA
Bitencourt, N. V., Righetto, G. M., Camargo, I. L. B. da C., Godoy, M. O. de, Guido, R. V. C., Oliva, G., et al. (2023). 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. Pharmaceutics, 15( 2), 436-1-436-17 + supplementary materials: 1-8. doi:10.3390/pharmaceutics15020436 -
NLM
Bitencourt NV, Righetto GM, Camargo ILB da C, Godoy MO de, Guido RVC, Oliva G, Santos Filho NA, Cilli EM. 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 [Internet]. Pharmaceutics. 2023 ; 15( 2): 436-1-436-17 + supplementary materials: 1-8.[citado 2024 abr. 28 ] Available from: https://doi.org/10.3390/pharmaceutics15020436 -
Vancouver
Bitencourt NV, Righetto GM, Camargo ILB da C, Godoy MO de, Guido RVC, Oliva G, Santos Filho NA, Cilli EM. 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 [Internet]. Pharmaceutics. 2023 ; 15( 2): 436-1-436-17 + supplementary materials: 1-8.[citado 2024 abr. 28 ] Available from: https://doi.org/10.3390/pharmaceutics15020436 - Effect of dimerization on antibacterial and SARS-CoV-2 papain-like cysteine protease (PLpro) activity of the peptide (p-BthTX-I)
- Effect of C-terminal and N-terminal dimerization and alanine scan on antibacterial activity of the analogs of the peptide p-BthTX-I
- Evaluation of the antimicrobial activity of bothropstoxin-I derivative peptide as an alternative molecule against multidrugresistant bacteria
- Effect of C-terminal and N-terminal dimerization and alanine scanning on antibacterial activity of the analogs of the peptide p-BthTX-I
- Activity of fractions obtained from extract of Fusarium oxysporum isolated from Senna spectabilis against Staphylococcus epidermidis in biofilm and planktonic forms
- Antibacterial activity optimization of peptides originating from Bothropstoxin-I
- Synthesis of boronic acid derivatives designed as SARS-CoV-2 MPro inhibitors
- Discovery of RNA-dependent RNA polymerase complex (RDRP) inhibitors from SARS-COV-2 as hits for COVID-19 drug development
- Descoberta de inibidores do complexo RNA polimerase dependente de RNA (RdRp) de SARS-CoV-2 como candidatos a compostos líderes para covid-19
- Structural study of the Staphylococcus aureus regulatory protein GraR
Informações sobre o DOI: 10.3390/pharmaceutics15020436 (Fonte: oaDOI API)
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