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Antibacterial Activity of the Non-Cytotoxic Peptide (p-BthTX-I)2 and Its Serum Degradation Product against Multidrug-Resistant Bacteria.
Santos-Filho, Norival A; Fernandes, Rafaela S; Sgardioli, Bruna F; Ramos, Matheus A S; Piccoli, Julia P; Camargo, Ilana L B C; Bauab, Tais M; Cilli, Eduardo M.
Afiliação
  • Santos-Filho NA; Instituto de Química, Universidade Estadual Paulista (UNESP), Araraquara-SP 14800-060, Brazil. drnorival@yahoo.com.
  • Fernandes RS; Instituto de Física de São Carlos, USP-Universidade de São Paulo, São Carlos-SP 13563-120, Brazil. rafaela.fernandes@usp.br.
  • Sgardioli BF; Instituto de Física de São Carlos, USP-Universidade de São Paulo, São Carlos-SP 13563-120, Brazil. sgardiolibruna@yahoo.com.br.
  • Ramos MAS; Faculdade de Ciências Farmacêuticas, Universidade Estadual Paulista (UNESP), Araraquara-SP 14800-903, Brazil. matheusramos_91@hotmail.com.
  • Piccoli JP; Instituto de Química, Universidade Estadual Paulista (UNESP), Araraquara-SP 14800-060, Brazil. juliappiccoli@gmail.com.
  • Camargo ILBC; Instituto de Física de São Carlos, USP-Universidade de São Paulo, São Carlos-SP 13563-120, Brazil. ilanacamargo@ifsc.usp.br.
  • Bauab TM; Faculdade de Ciências Farmacêuticas, Universidade Estadual Paulista (UNESP), Araraquara-SP 14800-903, Brazil. tmbauab@gmail.com.
  • Cilli EM; Instituto de Química, Universidade Estadual Paulista (UNESP), Araraquara-SP 14800-060, Brazil. eduardocilli@gmail.com.
Molecules ; 22(11)2017 Nov 04.
Article em En | MEDLINE | ID: mdl-29113051
ABSTRACT
Antimicrobial peptides can be used systemically, however, their susceptibility to proteases is a major obstacle in peptide-based therapeutic development. In the present study, the serum stability of p-BthTX-I (KKYRYHLKPFCKK) and (p-BthTX-I)2, a p-BthTX-I disulfide-linked dimer, were analyzed by mass spectrometry and analytical high-performance liquid chromatography (HPLC). Antimicrobial activities were assessed by determining their minimum inhibitory concentrations (MIC) using cation-adjusted Mueller-Hinton broth. Furthermore, biofilm eradication and time-kill kinetics were performed. Our results showed that p-BthTX-I and (p-BthTX-I)2 were completely degraded after 25 min. Mass spectrometry showed that the primary degradation product was a peptide that had lost four lysine residues on its C-terminus region (des-Lys12/Lys13-(p-BthTX-I)2), which was stable after 24 h of incubation. The antibacterial activities of the peptides p-BthTX-I, (p-BthTX-I)2, and des-Lys12/Lys13-(p-BthTX-I)2 were evaluated against a variety of bacteria, including multidrug-resistant strains. Des-Lys12/Lys13-(p-BthTX-I)2 and (p-BthTX-I)2 degraded Staphylococcus epidermidis biofilms. Additionally, both the peptides exhibited bactericidal activities against planktonic S. epidermidis in time-kill assays. The emergence of bacterial resistance to a variety of antibiotics used in clinics is the ultimate challenge for microbial infection control. Therefore, our results demonstrated that both peptides analyzed and the product of proteolysis obtained from (p-BthTX-I)2 are promising prototypes as novel drugs to treat multidrug-resistant bacterial infections.
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Texto completo: 1 Base de dados: MEDLINE Assunto principal: Staphylococcus epidermidis / Biofilmes / Peptídeos Catiônicos Antimicrobianos / Farmacorresistência Bacteriana Múltipla / Antibacterianos Limite: Humans / Male Idioma: En Revista: Molecules Assunto da revista: BIOLOGIA Ano de publicação: 2017 Tipo de documento: Article País de afiliação: Brasil

Texto completo: 1 Base de dados: MEDLINE Assunto principal: Staphylococcus epidermidis / Biofilmes / Peptídeos Catiônicos Antimicrobianos / Farmacorresistência Bacteriana Múltipla / Antibacterianos Limite: Humans / Male Idioma: En Revista: Molecules Assunto da revista: BIOLOGIA Ano de publicação: 2017 Tipo de documento: Article País de afiliação: Brasil