2014, Number 6
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Rev Invest Clin 2014; 66 (6)
In vitro determination of the short-chain synthetic peptide RP13 antimicrobial activity
Sánchez A, Calderón E, Castañón-Alonso SL, Santos A, Hernández B, Vázquez A
Language: English
References: 37
Page: 527-533
PDF size: 159.11 Kb.
ABSTRACT
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 gramnegative
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.
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