Synthetic Peptides Derived from Bovine Lactoferricin Exhibit Antimicrobial Activity against E. coli ATCC 11775, S. maltophilia ATCC 13636 and S. enteritidis ATCC 13076
Nataly De Jesús Huertas Méndez,
Yerly Vargas Casanova,
Anyelith Katherine Gómez Chimbi,
Edith Hernández,
Aura Lucia Leal Castro,
Javier Mauricio Melo Diaz,
Zuly Jenny Rivera Monroy,
Javier Eduardo García Castañeda
Affiliations
Nataly De Jesús Huertas Méndez
Chemistry Department, Universidad Nacional de Colombia, Bogotá Carrera 45 No 26-85, Building 451, office 409, Bogotá 11321, Colombia
Yerly Vargas Casanova
Bacteriology Department, Universidad Colegio Mayor de Cundinamarca, Bogotá Calle 28 No. 5B-02, Bogotá 110311; Colombia
Anyelith Katherine Gómez Chimbi
Bacteriology Department, Universidad Colegio Mayor de Cundinamarca, Bogotá Calle 28 No. 5B-02, Bogotá 110311; Colombia
Edith Hernández
Bacteriology Department, Universidad Colegio Mayor de Cundinamarca, Bogotá Calle 28 No. 5B-02, Bogotá 110311; Colombia
Aura Lucia Leal Castro
Medicine Faculty, Universidad Nacional de Colombia, Bogotá Carrera 45 No 26-85, Building 471, Bogotá 11321, Colombia
Javier Mauricio Melo Diaz
Chemistry Department, Universidad Nacional de Colombia, Bogotá Carrera 45 No 26-85, Building 451, office 409, Bogotá 11321, Colombia
Zuly Jenny Rivera Monroy
Chemistry Department, Universidad Nacional de Colombia, Bogotá Carrera 45 No 26-85, Building 451, office 409, Bogotá 11321, Colombia
Javier Eduardo García Castañeda
Pharmacy Department, Universidad Nacional de Colombia, Bogotá Carrera 45 No 26-85, Building 450, office 203, Bogotá 11321, Colombia
Linear, dimeric, tetrameric, and cyclic peptides derived from lactoferricin B–containing non-natural amino acids and the RWQWR motif were synthesized, purified, and characterized using RP-HPLC, MALDI-TOF mass spectrometry, and circular dichroism. The antibacterial activity of peptides against Escherichia coli ATCC 11775, Stenotrophomonas maltophilia ATCC 13636, and Salmonella enteritidis ATCC 13076 was evaluated. The minimum inhibitory concentration (MIC) and minimum bactericidal concentration (MBC) were determined. The synthetic bovine lactoferricin exhibited antibacterial activity against E. coli ATCC 11775 and S. enteritidis ATCC 13076. The dimeric peptide (RRWQWR)2K-Ahx exhibited the highest antibacterial activity against the tested bacterial strain. The monomeric, cyclic, tetrameric, and palindromic peptides containing the RWQWR motif exhibited high and specific activity against E. coli ATCC 11775. The results suggest that short peptides derived from lactoferricin B could be considered as potential candidates for the development of antibacterial agents against infections caused by E. coli.
