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Título: | Antimicrobial peptides and their superior fluorinated analogues: structure-activity relationships as revealed by NMR spectroscopy and MD calculations |
Autor: | Díaz, Dolores CSIC ORCID; Palomino-Schätzlein, M.; Corzana, Francisco; Andreu, C.; Carbajo, Rodrigo J.; Olmo, M. del; Canales, Ángeles CSIC ORCID; Pineda-Lucena, Antonio CSIC ORCID; Asensio, Gregorio; Jiménez-Barbero, Jesús CSIC ORCID | Palabras clave: | peptides Antimicrobial fluorine membranes molecular dynamics NMR spectroscopy |
Fecha de publicación: | 22-nov-2010 | Editor: | Wiley-VCH | Citación: | ChemBioChem; 11(17) : 2424-32 (2010) | Resumen: | The conformations of two synthetic pentapeptides with antimicrobial activity and their 4-fluorophenylalanine (Pff)-containing analogues (ArXArXAr-NH2; Ar=Phe, Pff; X=Lys, Arg) have been studied. NMR experiments carried out both in aqueous fluoroalcohol solutions and SDS micelles permitted their interactions with membrane-like environments to be explored. WaterLOGSY experiments and Mn2+-based paramagnetic probes were also applied to assess their orientations with respect to the SDS micelles. In addition, pulse-field gradient (PFG) diffusion NMR spectroscopy studies were conducted, under different experimental conditions (i.e., concentration, temperature) to characterize the possible changes in the peptides' aggregation states as a putative critical factor for their antimicrobial activity. Finally, molecular dynamics simulations on a variety of conformations showed the intrinsic flexibility of these peptides in both aqueous solutions and membrane-mimetic systems | Descripción: | 9 pag., 6 fig, 3 tab. | Versión del editor: | http://dx.doi.org/10.1002/cbic.201000424 | URI: | http://hdl.handle.net/10261/52669 | DOI: | 10.1002/cbic.201000424 | ISSN: | 1439-4227 | E-ISSN: | 1439-7633 |
Aparece en las colecciones: | (CIB) Artículos |
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