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Título

Role of positional hydrophobicity in the leishmanicidal activity of magainin 2

Autor Guerrero, Esther; Saugar, José María; Katsumi, Matsuzaki; Rivas, Luis
Fecha de publicación ago-2004
EditorAmerican Society for Microbiology
Citación Antimicrobial Agents and Chemotherapy 48: (8) 2980- 2986 (2004)
ResumenThe emergence of membrane-active antimicrobial peptides as new alternatives against pathogens with multiantibiotic resistance requires the design of better analogues. Among the different physicochemical parameters involved in the optimization of linear antimicrobial peptides, positional hydrophobicity has recently been incorporated. This takes into consideration the concept of the topological distribution of hydrophobic residues throughout the sequence rather than the classical concept of hydrophobicity as a global parameter of the peptide, calculated as the summation of the individual hydrophobicities of the residues. In order to assess the contribution of this parameter to the leishmanicidal mechanisms of magainin 2 analogues, the activities of two of these analogues, MG-H1 (GIKKFLHIIWKFIKAFVGEIMNS) and MG-H2 (IIKKFLHSIWKFGKAFVG EIMNI), which have similar charges, amino acid compositions, and hydrophobicities but different positional hydrophobicities, against Leishmania donovani promastigotes were assayed (T. Tachi, R. F. Epand, R. M. Epand, and K. Matsuzaki, Biochemistry 41:10723-10731, 2002). The activities were compared with that of the parental peptide, F5W-magainin 2 (GIGKWLHSAKKFGKAFVGEIMNS). The three peptides were active at micromolar concentrations, in the order MG-H2 > MG-H1 > FSW-magainin 2. These activities differ from their hemolytic and bactericidal activities. The results demonstrate that positional hydrophobicity, which reflects the presence of short stretches of sequences rich in hydrophobic amino acids, plays an important role in the activities of leishmanicidal peptides.
Versión del editorhttp://dx.doi.org/10.1128/AAC.48.8.2980-2986.2004
URI http://hdl.handle.net/10261/97018
DOI10.1128/AAC.48.8.2980-2986.2004
ISSN0066-4804
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