Next Article in Journal
In Vitro Antimicrobial Activity of Various Cefoperazone/Sulbactam Products
Next Article in Special Issue
A Rapid Fluorescence-Based Microplate Assay to Investigate the Interaction of Membrane Active Antimicrobial Peptides with Whole Gram-Positive Bacteria
Previous Article in Journal
Characterization and Antimicrobial Activity of the Teleost Chemokine CXCL20b
Previous Article in Special Issue
Trematocine, a Novel Antimicrobial Peptide from the Antarctic Fish Trematomus bernacchii: Identification and Biological Activity
Article

Ib-M6 Antimicrobial Peptide: Antibacterial Activity against Clinical Isolates of Escherichia coli and Molecular Docking

1
Facultad de Ciencias Exactas, Naturales y Agropecuarias, Ciencias Básicas Aplicadas para la Sostenibilidad—CIBAS, Universidad de Santander, Calle 70 No. 55-210, C.P. Bucaramanga (Santander) 680003, Colombia
2
Facultad de Ciencias de la Salud, Grupo de Investigación en Biología Molecular y Biotecnología, Universidad de Santander, Calle 70 No. 55-210, C.P. 680003 Bucaramanga (Santander), Colombia
3
Facultad de Ciencias de la Salud, Grupo de Investigación en Manejo Clínico—CliniUdes, Universidad de Santander, Calle 70 No. 55-210, C.P. 680003 Bucaramanga (Santander), Colombia
4
Division of Pediatric Infectious Diseases, Department of Pediatrics, Jacobs School of Medicine and Biomedical Sciences, University at Buffalo, Buffalo, NY 14203, USA
*
Authors to whom correspondence should be addressed.
Antibiotics 2020, 9(2), 79; https://doi.org/10.3390/antibiotics9020079
Received: 28 November 2019 / Revised: 27 December 2019 / Accepted: 8 January 2020 / Published: 12 February 2020
(This article belongs to the Special Issue Antibacterial Peptides)
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
Keywords: antimicrobial peptides; Escherichia coli; molecular docking antimicrobial peptides; Escherichia coli; molecular docking
Show Figures

Figure 1

MDPI and ACS Style

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, O.G. Ib-M6 Antimicrobial Peptide: Antibacterial Activity against Clinical Isolates of Escherichia coli and Molecular Docking. Antibiotics 2020, 9, 79. https://doi.org/10.3390/antibiotics9020079

AMA Style

Flórez-Castillo JM, Rondón-Villareal P, Ropero-Vega JL, Mendoza-Espinel SY, Moreno-Amézquita JA, Méndez-Jaimes KD, Farfán-García AE, Gómez-Rangel SY, Gómez-Duarte OG. Ib-M6 Antimicrobial Peptide: Antibacterial Activity against Clinical Isolates of Escherichia coli and Molecular Docking. Antibiotics. 2020; 9(2):79. https://doi.org/10.3390/antibiotics9020079

Chicago/Turabian Style

Flórez-Castillo, J. M., P. Rondón-Villareal, J. L. Ropero-Vega, S. Y. Mendoza-Espinel, J. A. Moreno-Amézquita, K. D. Méndez-Jaimes, A. E. Farfán-García, S. Y. Gómez-Rangel, and Oscar G. Gómez-Duarte 2020. "Ib-M6 Antimicrobial Peptide: Antibacterial Activity against Clinical Isolates of Escherichia coli and Molecular Docking" Antibiotics 9, no. 2: 79. https://doi.org/10.3390/antibiotics9020079

Find Other Styles
Note that from the first issue of 2016, MDPI journals use article numbers instead of page numbers. See further details here.

Article Access Map by Country/Region

1
Back to TopTop