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PublicationBiopolymers
Year2014
Volume101
Pages319–328,
International

DESIGN AND ACTIVITY OF NOVEL LACTOFERRAMPIN ANALOGS AGAINST O157:H7 ENTEROHAEMORRHAGIC Escherichia coli

Authors:Roberto Fernandez-Lafuente
Groups of research:Optimización de biocatalizadores y bioprocesos enzimáticos
Jenniffer Cruz a, Claudia C. Ortiz b, Fanny Guzmán c, Constanza Cárdenasc , Roberto Fernandez-Lafuente*d and Rodrigo G. Torresa*.
aGrupo de Investigación en Bioquímica y Microbiología (GIBIM), Escuela de Química, Universidad Industrial de Santander, Edificio Camilo Torres 202, Bucaramanga, Colombia
bGrupo de Investigación en Bioquímica y Microbiología (GIBIM), Escuela de Bacteriología y Laboratorio Clínico, Universidad Industrial de Santander, Edificio Camilo Torres 202, Bucaramanga, Colombia.
cNBC Núcleo Biotecnología Curauma, Pontificia Universidad Católica de Valparaíso, Campus Curauma, Av. Universidad, 330 Valparaíso, Chile.
d Departamento de Biocatálisis. ICP-CSIC, Campus UAM-CSIC Cantoblanco, Madrid. Spain

Lactoferrampin 265-284 (LFampin 265-284) is a peptide consisting of residues 265-284 of N1-domain of bovine Lactoferrin (LF). This peptide has several cationic groups in the C-terminal lobe, exhibiting an antibacterial activity against a wide range of microorganisms. However, LFampin 265-284 exhibits low antimicrobial activity against the O157:H7 enterohaemorrhagic Escherichia coli (EHEC O157:H7) when compared to Lactoferrin chimera and Lactoferricin. Here, we have designed three analogues of LFampin 265-284 based on the distribution of cationic groups, hydrophobicity, size and sequence. Analogues were synthesized by solid phase chemistry using Fmoc methodology obtaining peptides with 95% purity. All peptides maintain the ability to adopt helical conformations (checked by circular dichroism spectra and molecular simulations). Some of these analogues exhibited a significant increase in antimicrobial activity by counting colony forming units against EHEC O157:H7 compared to native LFampin 265-284, with MIC of 10 and 40 µM for 264G-D265K and 264G-D265K/S272R, respectively. The incorporation of a GKLI sequence in the N-terminal lobe increased dramatically its antibacterial activity, an effect which has been attributed to the addition of cationic groups in the N-terminal side that may stabilize the helical conformation of the new designed peptides. 
Keywords:peptide design, antimicrobial peptides, bovine lactoferrampin, synthetic peptides, EHEC O157:H7.
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