Please use this identifier to cite or link to this item: https://repositorio.udes.edu.co/handle/001/5665
Title: Ib-M6 antimicrobial peptide: Antibacterial activity against clinical isolates of Escherichia coli and molecular docking
Authors: Flórez Castillo, Johanna-Marcela
Rondón Villarreal, Paola
Ropero Vega, José Luis
Mendoza Espinel, Stephany Y.
Moreno Amézquita, July A.
Méndez Jaimes, Karen D.
Farfán García, Ana Elvira
Gómez Rangel, Sergio-Yebrail
Gómez Duarte, Oscar Gilberto
Keywords: Antimicrobial peptides
Escherichia coli
Molecular docking
Issue Date: 12-Mar-2020
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. View Full-Text
Description: Digital
Source: https://www.mdpi.com/2079-6382/9/2/79#framed_div_cited_count
URI: https://repositorio.udes.edu.co/handle/001/5665
Appears in Collections:DCACA. Artículos de Investigación



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