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Molecules 2017, 22(6), 987; doi:10.3390/molecules22060987

Antimicrobial Activity of Truncated and Polyvalent Peptides Derived from the FKCRRQWQWRMKKGLA Sequence against Escherichia coli ATCC 25922 and Staphylococcus aureus ATCC 25923

1
Chemistry Department, Universidad Nacional de Colombia, Bogotá Carrera 45 No. 26-85, Building 451, Office 409, Laboratory 334, Bogotá 11321, Colombia
2
Pharmacy Department, Universidad Nacional de Colombia, Bogotá Carrera 45 No. 26-85, Building 450, office 203, Bogotá 11321, Colombia
*
Author to whom correspondence should be addressed.
Received: 29 April 2017 / Revised: 8 June 2017 / Accepted: 12 June 2017 / Published: 14 June 2017
(This article belongs to the Special Issue Peptide-Based Drugs and Drug Delivery Systems)
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Abstract

Peptides derived from LfcinB were designed and synthesized, and their antibacterial activity was tested against Escherichia coli ATCC 25922 and Staphylococcus aureus ATCC 25923. Specifically, a peptide library was constructed by systemically removing the flanking residues (N or C-terminal) of Lfcin 17–31 (17FKCRRWQWRMKKLGA31), maintaining in all peptides the 20RRWQWR25 sequence that corresponds to the minimal antimicrobial motif. For this research, also included were (i) a peptide containing an Ala instead of Cys ([Ala19]-LfcinB 17–31) and (ii) polyvalent peptides containing the RRWQWR sequence and a non-natural amino acid (aminocaproic acid). We established that the lineal peptides LfcinB 17–25 and LfcinB 17–26 exhibited the greatest activity against E. coli ATCC 25922 and S. aureus ATCC 25923, respectively. On the other hand, polyvalent peptides, a dimer and a tetramer, exhibited the greatest antibacterial activity, indicating that multiple copies of the sequence increase the activity. Our results suggest that the dimeric and tetrameric sequence forms potentiate the antibacterial activity of lineal sequences that have exhibited moderate antibacterial activity. View Full-Text
Keywords: Keywords: bovine lactoferricin; antibacterial activity; synthetic peptides; branched peptides; E. coli; S. aureus Keywords: bovine lactoferricin; antibacterial activity; synthetic peptides; branched peptides; E. coli; S. aureus
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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).

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MDPI and ACS Style

Huertas, N.J.; Monroy, Z.J.R.; Medina, R.F.; Castañeda, J.E.G. Antimicrobial Activity of Truncated and Polyvalent Peptides Derived from the FKCRRQWQWRMKKGLA Sequence against Escherichia coli ATCC 25922 and Staphylococcus aureus ATCC 25923. Molecules 2017, 22, 987.

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