In vitro determination of the short-chain synthetic peptide RP 13 antimicrobial activity
Por:
Sánchez A., Calderón E., Castañon-Alonso S.L., Santos A., Hernández B., Vázquez A.
Publicada:
1 nov 2014
Categoría:
Medicine (miscellaneous)
Resumen:
Background. The proliferation of antibiotic-resistant microorganisms,
along with the lack of new drugs against them, has elicited the interest
of the scientific community on the study and development of endogenous
synthetic compounds with bacteriostatic or bactericidal activity. In
recent years, several short-chain, low molecular weight peptides
isolated from natural sources such as plants and animals have
demonstrated an array of antimicrobial activities. Despite having
structural characteristics similar to microbicidal peptides isolated
from human platelets, peptide RP11 does not exhibit antimicrobial
activity. Objective. In vitro determination of the antimicrobial
activity of the synthetic peptide RP13. Material and methods. Peptide
RP13 was prepared modifying the original amino acids sequence of peptide
RP11, reversing the position of the amino acids lysine and tyrosine in
order to modify the conformation of the original peptide. These amino
acids are localized close to the N-terminus of the peptidic chain.
Peptide RP13 was prepared in solution using conventional methods for
peptide synthesis. The antimicrobial activity of RP13 was assessed
against the microorganisms S. aureus, E. faecalis and E. coli in a test
solution and later evaluated by cultivation of plates during the first 2
h after inoculation of bacteria. RP13 activity antimicrobial was
compared against tetracycline, a broad-spectrum antibiotic. Results. The
new peptide RP13, resulting form the structural modification of the
amino acid sequence of peptide RP11, displayed antimicrobial activity.
RP13 demonstrated to be more efficient inhibiting the growth of
gram-positive than gram-negative bacteria. Conclusions. The structural
modification of peptide RP11, obtained from human platelets, resulted in
a new peptide with improved antimicrobial activity. These results
clearly demonstrate that peptides of natural origin, as well as their
synthetic analogs, represent an attractive alternative against
pathogenic agents.
Filiaciones:
Sánchez A.:
Laboratorio de Inmunoquímica, Hospital Infantil de México Federico Gómez, Dr. Márquez No. 162, Col. Doctores, México, D.F., 06720, Mexico
Calderón E.:
Laboratorio de Inmunoquímica, Hospital Infantil de México Federico Gómez, Dr. Márquez No. 162, Col. Doctores, México, D.F., 06720, Mexico
Castañon-Alonso S.L.:
Laboratorio de Inmunoquímica, Hospital Infantil de México Federico Gómez, Dr. Márquez No. 162, Col. Doctores, México, D.F., 06720, Mexico
Santos A.:
Laboratorio de Inmunoquímica, Hospital Infantil de México Federico Gómez, Dr. Márquez No. 162, Col. Doctores, México, D.F., 06720, Mexico
Hernández B.:
Laboratorio de Inmunoquímica, Hospital Infantil de México Federico Gómez, Dr. Márquez No. 162, Col. Doctores, México, D.F., 06720, Mexico
Vázquez A.:
Departamento de Química Orgánica, Facultad de Química, Universidad Nacional Autónoma de México, Mexico
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