Next Article in Journal
Evaluation of Maltose-Based Cationic Liposomes with Different Hydrophobic Tails for Plasmid DNA Delivery
Next Article in Special Issue
Screening, Purification and Characterization of Anionic Antimicrobial Proteins from Foeniculum Vulgare
Previous Article in Journal
Chemical Constituents of Smilax china L. Stems and Their Inhibitory Activities against Glycation, Aldose Reductase, α-Glucosidase, and Lipase
Previous Article in Special Issue
β-Defensins in the Fight against Helicobacter pylori
Article Menu
Issue 3 (March) cover image

Export Article

Open AccessArticle
Molecules 2017, 22(3), 452; doi:10.3390/molecules22030452

Synthetic Peptides Derived from Bovine Lactoferricin Exhibit Antimicrobial Activity against E. coli ATCC 11775, S. maltophilia ATCC 13636 and S. enteritidis ATCC 13076

1
Chemistry Department, Universidad Nacional de Colombia, Bogotá Carrera 45 No 26-85, Building 451, office 409, Bogotá 11321, Colombia
2
Bacteriology Department, Universidad Colegio Mayor de Cundinamarca, Bogotá Calle 28 No. 5B-02, Bogotá 110311; Colombia
3
Medicine Faculty, Universidad Nacional de Colombia, Bogotá Carrera 45 No 26-85, Building 471, Bogotá 11321, Colombia
4
Pharmacy Department, Universidad Nacional de Colombia, Bogotá Carrera 45 No 26-85, Building 450, office 203, Bogotá 11321, Colombia
These authors contributed equally to this work.
*
Author to whom correspondence should be addressed.
Academic Editors: Paula A. C. Gomes and Stefania Galdiero
Received: 7 February 2017 / Revised: 1 March 2017 / Accepted: 8 March 2017 / Published: 12 March 2017
(This article belongs to the Special Issue Peptide-Based Drugs and Drug Delivery Systems)
View Full-Text   |   Download PDF [1181 KB, uploaded 12 March 2017]   |  

Abstract

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. View Full-Text
Keywords: Lactoferricin B; E. coli; S. maltophilia; S. enteritidis; antibacterial activity; synthetic peptides Lactoferricin B; E. coli; S. maltophilia; S. enteritidis; antibacterial activity; synthetic peptides
Figures

Figure 1

This is an open access article distributed under the Creative Commons Attribution License which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited. (CC BY 4.0).

Scifeed alert for new publications

Never miss any articles matching your research from any publisher
  • Get alerts for new papers matching your research
  • Find out the new papers from selected authors
  • Updated daily for 49'000+ journals and 6000+ publishers
  • Define your Scifeed now

SciFeed Share & Cite This Article

MDPI and ACS Style

Huertas Méndez, N.D.J.; Vargas Casanova, Y.; Gómez Chimbi, A.K.; Hernández, E.; Leal Castro, A.L.; Melo Diaz, J.M.; Rivera Monroy, Z.J.; García Castañeda, J.E. Synthetic Peptides Derived from Bovine Lactoferricin Exhibit Antimicrobial Activity against E. coli ATCC 11775, S. maltophilia ATCC 13636 and S. enteritidis ATCC 13076. Molecules 2017, 22, 452.

Show more citation formats Show less citations formats

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

Related Articles

Article Metrics

Article Access Statistics

1

Comments

[Return to top]

Molecules EISSN 1420-3049 Published by MDPI AG, Basel, Switzerland RSS E-Mail Table of Contents Alert
Back to Top