TY  - JOUR
A1  - León-Calvijo, María A.
A1  - Leal-Castro, Aura L.
A1  - Almanzar-Reina, Giovanni A.
A1  - Rosas-Pérez, Jaiver E.
A1  - García-Castañeda, Javier E.
A1  - Rivera-Monroy, Zuly J.
T1  - Antibacterial activity of synthetic peptides derived from lactoferricin against Escherichia coli ATCC 25922 and Enterococcus faecalis ATCC 29212
JF  - BioMed Research International
N2  - 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 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.
KW  - bovine lactoferricin
KW  - antimicrobial activity
KW  - infection
KW  - spectrum
KW  - mice
KW  - cells
KW  - inhibit
KW  - derivatives
KW  - loop region
Y1  - 2015
U6  - http://nbn-resolving.de/urn/resolver.pl?urn:nbn:de:bvb:20-opus-144591
IS  - 453826
ER  -