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scopus(4)
Lysine N <sup>ε</sup>-trimethylation, a tool for improving the selectivity of antimicrobial peptides
ArticleAbstract: The effects of lysine N?-trimethylation at selected positions of the antimicrobial cecropin A?melittPalabras claves:Autores:Andreu D., B. G. De la Torre, Cabrales-Rico A., Díaz D., Fernández-Reyes M., Jiménez-Barbero J., Rivas L., Vallès-Miret M.Fuentes:scopusSequence inversion and phenylalanine surrogates at the β-Turn enhance the antibiotic activity of gramicidin S
ArticleAbstract: A series of gramicidin S (GS) analogues have been synthesized where the Phe (i + 1) and Pro (i + 2)Palabras claves:Autores:Andreu D., B. G. De la Torre, Cativiela C., Fernández-Reyes M., Jiménez A.I., Jiménez M.A., Rivas L., Santiveri C.M., Solanas C.Fuentes:scopusStructural framework for the modulation of the activity of the hybrid antibiotic peptide cecropin A-melittin [CA(1-7)M(2-9)] by N <sup>ε</sup>-lysine trimethylation
ArticleAbstract: The 3D structures of six linear pentadecapeptides derived from the cecropin A-melittin antimicrobialPalabras claves:Antimicrobial peptides (AMPs), cecropin A, membranes, NMR spectroscopy, TrimethyllysineAutores:Andreu D., B. G. De la Torre, Díaz M.D., Fernández-Reyes M., Jiménez-Barbero J., Rivas L.Fuentes:scopusTherapeutic index of gramicidin S is strongly modulated by D-phenylalanine analogues at the β-turn
ArticleAbstract: Analogues of the cationic antimicrobial peptide gramicidin S (GS), cyclo(Val-Orn-Leu-D-Phe-Pro)2, wiPalabras claves:Autores:Andreu D., B. G. De la Torre, Cativiela C., Fernández-Reyes M., Jiménez A.I., Jiménez M.A., Rivas L., Santiveri C.M., Solanas C.Fuentes:scopus