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  - 
TY  - JOUR
A1  - Vargas Casanova, Yerly
A1  - Rodríguez Guerra, Jorge Antonio
A1  - Umaña Pérez, Yadi Adriana
A1  - Leal Castro, Aura Lucía
A1  - Almanzar Reina, Giovanni
A1  - García Castañeda, Javier Eduardo
A1  - Rivera Monroy, Zuly Jenny
T1  - Antibacterial synthetic peptides derived from bovine lactoferricin exhibit cytotoxic effect against MDA-MB-468 and MDA-MB-231 breast cancer cell lines
JF  - Molecules
N2  - Linear, dimeric, tetrameric, and cyclic peptides derived from lactoferricin B, containing the RRWQWR motif, were designed, synthesized, purified, and characterized using RP-HPLC chromatography and MALDI-TOF mass spectrometry. The antibacterial activity of the designed peptides against E. coli (ATCC 11775 and 25922) and their cytotoxic effect against MDA-MB-468 and MDA-MB-231 breast cancer cell lines were evaluated. Dimeric and tetrameric peptides showed higher antibacterial activity in both bacteria strains than linear peptides. The dimeric peptide (RRWQWR)\(_2\)K-Ahx exhibited the highest antibacterial activity against the tested bacterial strains. Furthermore, the peptides with high antibacterial activity exhibited significant cytotoxic effect against the tested breast cancer cell lines. This cytotoxic effect was fast and dependent on the peptide concentration. The tetrameric molecule containing RRWQWR motif has an optimal cytotoxic effect at a concentration of 22 µM. The evaluated dimeric and tetrameric peptides could be considered as candidates for developing new therapeutic agents against breast cancer. Polyvalence of linear sequences could be considered as a novel and versatile strategy for obtaining molecules with high anticancer activity.
KW  - lactoferricin B
KW  - E. coli
KW  - breast cancer
KW  - cytotoxic effect
KW  - antibacterial activity
KW  - synthetic peptides
Y1  - 2017
U6  - http://nbn-resolving.de/urn/resolver.pl?urn:nbn:de:bvb:20-opus-173887
VL  - 22
IS  - 10
ER  -