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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) 4 K 2   Ahx   2 C 2 ) exhibit bigger or similar activity against  E. coli  (MIC 4–33  μ M) and  E. faecalis  (MIC 10–33  μ M) 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.

biomed research international

Antibacterial Activity of Synthetic Peptides Derived from Lactoferricin against<i>Escherichia coli</i>ATCC 25922 and<i>Enterococcus faecalis</i>ATCC 29212

Antibacterial Activity of Synthetic Peptides Derived from Lactoferricin againstEscherichia coliATCC 25922 andEnterococcus faecalisATCC 29212