Structural and antimicrobial properties of human pre-elafin/trappin-2 and derived peptides against Pseudomonas aeruginosa |
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| Authors: | Audrey Bellemare Nathalie Vernoux Sébastien Morin Stéphane M Gagné Yves Bourbonnais |
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| Affiliation: | 1.Département de biochimie, microbiologie et bio-informatique, Institut de biologie intégrative et des systèmes and Regroupement PROTEO,Université Laval,Québec,Canada;2.INAF, Département des sciences des aliments et de nutrition Faculté des sciences de l'agriculture et de l'alimentation Université Laval.,Québec,Canada;3.Division of Structural Biology, Biozentrum,University of Basel,Basel,Switzerland |
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| Abstract: | Background Pre-elafin/trappin-2 is a human innate defense molecule initially described as a potent inhibitor of neutrophil elastase. The full-length protein as well as the N-terminal "cementoin" and C-terminal "elafin" domains were also shown to possess broad antimicrobial activity, namely against the opportunistic pathogen P. aeruginosa. The mode of action of these peptides has, however, yet to be fully elucidated. Both domains of pre-elafin/trappin-2 are polycationic, but only the structure of the elafin domain is currently known. The aim of the present study was to determine the secondary structures of the cementoin domain and to characterize the antibacterial properties of these peptides against P. aeruginosa. |
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