TAILIEUCHUNG - Báo cáo khoa học: Structural requirements for antimicrobial versus chemoattractant activities for dermaseptin S9

Dermaseptin S9 (Drs S9), GLRSKIWLWVLLMIWQESNKFKKM, iso-lated from frog skin, does not resemble any of the cationic and amphipathic antimicrobial peptides identified to date, having a highly hydrophobic core sequence flanked at either side by cationic termini. | ễFEBS Journal Structural requirements for antimicrobial versus chemoattractant activities for dermaseptin S9 Constance Auvynet1 2 Chahrazade El Amri1 Claire Lacombe1 Francine Bruston1 Julie Bourdais2 Pierre Nicolas1 and Yvonne Rosenstein2 1 UPMC Université de Paris 06 CNRS FRE 2852 Peptidome de la Peau des Amphibiens Paris Cedex 5 France 2 Departamento de Medicina Molecular y Bioprocesos Instituto de Biotecnologia Universidad NacionalAutonoma de Mexico Cuernavaca Morelos Mexico Keywords antimicrobialpeptide chemotaxis dermaseptin frog skin infrared spectroscopy Correspondence P. Nicolas UPMC University Paris 06 CNRS FRE 2852 Peptidome de la Peau des Amphibiens Tour 43 2 place Jussieu 75251 Paris cedex 5 France Fax 33 1 44 27 59 94 Tel 33 1 44 27 95 36 E-mail pnicolas@ Y. Rosenstein Departamento de Medicina Molecular y Bioprocesos Instituto de Biotecnologia Universidad Nacional Autonoma de Mexico Avenida Universidad 2001 ColChamilpa Cuernavaca Mor. 62270 Mexico Fax 52 73172388 Tel 52 5 55 66 22 76 63 E-mail yvonne@ Received 29 April2008 revised 11 June 2008 accepted 16 June 2008 doi Dermaseptin S9 Drs S9 GLRSKIWLWVLLMIWQESNKFKKM isolated from frog skin does not resemble any of the cationic and amphipathic antimicrobial peptides identified to date having a highly hydrophobic core sequence flanked at either side by cationic termini. Previous studies Lequin O Ladram A Chabbert A Bruston F Convert O Vanhoye D Chassaing G Nicolas P Amiche M 2006 Biochemistry 45 468-480 demonstrated that this peptide adopted a non-amphipathic a-helical conformation in trifluoroethanol water mixtures but was highly aggregated in aqueous solutions and in the presence of sodium dodecyl sulfate micelles. Circular dichroism FTIR and attenuated total reflectance FTIR spectroscopies combined with a surface plasmon resonance study show that Drs S9 forms stable and ordered b-sheet aggregates in aqueous buffers or when bound to anionic or .

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