In vitro determination of the short-chain synthetic peptide RP 13 antimicrobial activity

被引:0
|
作者
Sanchez, Adrian [1 ]
Calderon, Ernesto [1 ]
Castanon-Alonso, Sandra L. [1 ]
Santos, Araceli [1 ]
Hernandez, Beatriz [1 ]
Vazquez, Alfredo [2 ]
机构
[1] Hosp Infantil Mexico Dr Federico Gomez, Lab Inmunoquim, Mexico City 06720, DF, Mexico
[2] Univ Nacl Autonoma Mexico, Fac Quim, Dept Quim Organ, Mexico City 04510, DF, Mexico
关键词
Antimicrobial peptides; Antimicrobial activity; Gram-negative; Gram-positive; Bacteria; Synthetic peptides; ANTIBACTERIAL ACTIVITY; ANTIBIOTICS; DEFENSINS; RESISTANCE; IMMUNITY; INNATE;
D O I
暂无
中图分类号
R5 [内科学];
学科分类号
1002 ; 100201 ;
摘要
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.
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页码:527 / 533
页数:7
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