Abstract
Peptides derived from human and bovine lactoferricin were designed, synthesized, purified, and characterized using RP-HPLC and MALDI-TOF-MS. Specific changes in the sequences were designed as (i) the incorporation of unnatural amino acids in the sequence, the (ii) reduction or (iii) elongation of the peptide chain length, and (iv) synthesis of molecules with different number of branches containing the same sequence. For each peptide, the antibacterial activity against Escherichia coli ATCC 25922 and Enterococcus faecalis ATCC 29212 was evaluated. Our results showed that Peptides I.2 (RWQWRWQWR) and I.4 ((RRWQWR)4K2 Ahx 2C2) exhibit bigger or similar activity against E. coli (MIC 4–33 μM) and E. faecalis (MIC 10–33 μM) when they were compared with lactoferricin protein (LF) and some of its derivate peptides as II.1 (FKCRRWQWRMKKLGA) and IV.1 (FKCRRWQWRMKKLGAPSITCVRRAE). It should be pointed out that Peptides I.2 and I.4, containing the RWQWR motif, are short and easy to synthesize; our results demonstrate that it is possible to design and obtain synthetic peptides that exhibit enhanced antibacterial activity using a methodology that is fast and low-cost and that allows obtaining products with a high degree of purity and high yield.
Highlights
The World Health Organization has stated that control and/or treatment of infections caused by bacteria resistant to conventional drugs is considered a public health goal [1]
minimum inhibitory concentration (MIC) and minimum bactericidal concentration (MBC) values obtained against E. coli ATCC 25922 showed that Peptides I.2 and I.4 (Table 1) have the highest antibacterial activity against this strain, MIC 4 and 27 μM, respectively
Peptide I has been considered as the minimum motif with antibacterial action, and its activity has been attributed to the presence of Trp and Arg residues in an alternating way
Summary
The World Health Organization has stated that control and/or treatment of infections caused by bacteria resistant to conventional drugs is considered a public health goal [1]. Antimicrobial peptides (AMPs) have received special attention as a possible alternative way to combat infections caused by antibiotic-resistant bacterial strains. AMPs have been identified in body fluid proteins in mammals [5], lactoferrin (LF), an 80 kDa nonheme iron-binding protein that is located in mucosal secretions such as breast milk, saliva, seminal plasma, and vaginal mucus [2, 3, 6].
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