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Molecules 2017, 22(11), 1898;

Antibacterial Activity of the Non-Cytotoxic Peptide (p-BthTX-I)2 and Its Serum Degradation Product against Multidrug-Resistant Bacteria

Instituto de Química, Universidade Estadual Paulista (UNESP), Araraquara-SP 14800-060, Brazil
Instituto de Física de São Carlos, USP—Universidade de São Paulo, São Carlos-SP 13563-120, Brazil
Faculdade de Ciências Farmacêuticas, Universidade Estadual Paulista (UNESP), Araraquara-SP 14800-903, Brazil
Authors to whom correspondence should be addressed.
Received: 3 October 2017 / Revised: 30 October 2017 / Accepted: 31 October 2017 / Published: 4 November 2017
(This article belongs to the Special Issue Peptide Therapeutics)
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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. View Full-Text
Keywords: (p-BthTX-I)2; multidrug-resistant bacteria; biofilm; antimicrobial peptides (p-BthTX-I)2; multidrug-resistant bacteria; biofilm; antimicrobial peptides

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Santos-Filho, N.A.; Fernandes, R.S.; Sgardioli, B.F.; Ramos, M.A.S.; Piccoli, J.P.; Camargo, I.L.B.C.; Bauab, T.M.; Cilli, E.M. Antibacterial Activity of the Non-Cytotoxic Peptide (p-BthTX-I)2 and Its Serum Degradation Product against Multidrug-Resistant Bacteria. Molecules 2017, 22, 1898.

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