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- Title
Ib-M6 Antimicrobial Peptide: Antibacterial Activity against Clinical Isolates of Escherichia coli and Molecular Docking.
- Authors
Flórez-Castillo, J. M.; Rondón-Villareal, P.; Ropero-Vega, J. L.; Mendoza-Espinel, S. Y.; Moreno-Amézquita, J. A.; Méndez-Jaimes, K. D.; Farfán-García, A. E.; Gómez-Rangel, S. Y.; Gómez-Duarte, Oscar Gilberto
- Abstract
The Ib-M6 peptide has antibacterial activity against non-pathogenic Escherichia coli K-12 strain. The first part of this study determines the antibacterial activity of Ib-M6 against fourteen pathogenic strains of E. coli O157:H7. Susceptibility assay showed that Ib-M6 had values of Minimum Inhibitory Concentration (MIC) lower than streptomycin, used as a reference antibiotic. Moreover, to predict the possible interaction between Ib-M6 and outer membrane components of E. coli, we used molecular docking simulations where FhuA protein and its complex with Lipopolysaccharide (LPS–FhuA) were used as targets of the peptide. FhuA/Ib-M6 complexes had energy values between −39.5 and −40.5 Rosetta Energy Units (REU) and only one hydrogen bond. In contrast, complexes between LPS–FhuA and Ib-M6 displayed energy values between −25.6 and −40.6 REU, and the presence of five possible hydrogen bonds. Hence, the antimicrobial activity of Ib-M6 peptide shown in the experimental assays could be caused by its interaction with the outer membrane of E. coli.
- Subjects
MOLECULAR docking; ESCHERICHIA coli; ANTIMICROBIAL peptides; HYDROGEN bonding; STREPTOMYCIN; ANTIBIOTICS
- Publication
Antibiotics (2079-6382), 2020, Vol 9, Issue 2, p79
- ISSN
2079-6382
- Publication type
Article
- DOI
10.3390/antibiotics9020079