TAILIEUCHUNG - Báo cáo khoa học: Salt-resistant homodimeric bactenecin, a cathelicidin-derived antimicrobial peptide

The cathelicidin antimicrobial peptide bactenecin is ab-hairpin molecule with a single disulfide bond and broad antimicrobial activity. The proform of bactenecin exists as a dimer, however, and it has been proposed that bactenecin is released as a dimer in vivo, although there has been little study of the dimeric form of bactenecin. | ỊFEBS Journal Salt-resistant homodimeric bactenecin a cathelicidin-derived antimicrobial peptide Ju Y. Lee1 Sung-Tae Yang1 3 Seung K. Lee1 Hyun H. Jung1 Song Y. Shin2 Kyung-Soo Hahm2 and Jae I. Kim1 1 Department of Life Science BioImaging Research Center Gwangju Institute of Science and Technology Korea 2 Department of Bio-Materials Graduate Schooland Research Center for Proteineous Materials Chosun University Gwangju Korea 3 Section on Membrane Biology Laboratory of Cellular and Molecular Biophysics NationalInstitute of Child Health and Human Development NationalInstitutes of Health Bethesda MD USA Keywords antimicrobial peptides bactenecin dimerization peptide-membrane interaction salt resistance Correspondence J. I. Kim Department of Life Science Gwangju Institute of Science and Technology Gwangju 500-712 Korea Fax 82 62 970 2484 Tel 82 62 970 2494 E-mail jikim@ Received 19 July 2007 revised 28 April 2008 accepted 4 June 2008 doi The cathelicidin antimicrobial peptide bactenecin is a b-hairpin molecule with a single disulfide bond and broad antimicrobial activity. The proform of bactenecin exists as a dimer however and it has been proposed that bactenecin is released as a dimer in vivo although there has been little study of the dimeric form of bactenecin. To investigate the effect of bacten-ecin dimerization on its biological activity we characterized the dimer s effect on phospholipid membranes the kinetics of its bactericidal activity and its salt sensitivity. We initially synthesized two bactenecin dimers antiparallel and parallel and two monomers b-hairpin and linear . Under oxidative folding conditions reduced linear bactenecin preferentially folded into a dimer forming a ladder-like structure via intermolecular disulfide bonding. As compared to the monomer the dimer had a greater ability to induce lysis of lipid bilayers and was more rapidly bactericidal. Interestingly the dimer retained antimicrobial activity at

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