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.

Highlights

  • According to the World Health Organization (WHO), pathogen resistance to conventional antibiotics is considered a global public health problem

  • The antibacterial activity of linear, dimeric, tetrameric, and cyclic peptides derived from LfcinB against S. maltophilia, E. coli and S. enteritidis was evaluated

  • We demonstrated that the RWQWR peptide (LfcinB 20–25) presents antibacterial activity against E. coli ATCC 25922 [39]. This result is in accordance with Strom et al, who reported that short peptides RWRWRW and RRRWWW exhibit the best antibacterial activity against this bacterial strain [19]

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Summary

Introduction

According to the World Health Organization (WHO), pathogen resistance to conventional antibiotics is considered a global public health problem. Typhimurium are the two most important serotypes of salmonellosis transmitted from animals to humans in most parts of the world Infections caused by these pathogens have exhibited a gradual decline in susceptibility to traditional antibiotics [6,7]. Some biological activities of BLF are: regulator of the immune system, anti-inflammatory, metal absorption and metabolism ( iron), procoagulant, granulopoesis, protease inhibitor, anticarcinogenic, and cellular proliferation and differentiation [12,13,14,15] This protein is part of the innate immune response, exhibiting antimicrobial activity against: parasites, viruses, fungi and Gram-positive and Gram-negative bacteria [12,14,16,17]. The antibacterial activity of linear, dimeric, tetrameric, and cyclic peptides derived from LfcinB against S. maltophilia, E. coli and S. enteritidis was evaluated.

Results and Discussion
Reagents and Materials
LfcinB-Derived Peptide Synthesis
Analytical Methods
Susceptibility Assays
Antibacterial Activity Assays
Hemolytic Activity Assay
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