tailieunhanh - Báo cáo khoa học: Contribution of a central proline in model amphipathic a-helical peptides to self-association, interaction with phospholipids, and antimicrobial mode of action

Model amphipathic peptides have been widely used as a tool to determine the structural and biological properties that control the interaction of pep-tides with membranes. Here, we have focused on the role of a central Pro in membrane-active peptides. To determine the role of Pro in structure, antibiotic activity, and interaction with phospholipids, we generated a ser-ies of model amphipathic a-helical peptides with different chain lengths and containing or lacking a single central Pro. | ễFEBS Journal Contribution of a central proline in model amphipathic a-helical peptides to self-association interaction with phospholipids and antimicrobial mode of action Sung-Tae Yang1 Ju Yeon Lee1 Hyun-Jin Kim1 Young-Jae Eu1 Song Yub Shin2 Kyung-Soo Hahm2 and Jae Il Kim1 1 Department of Life Science Gwangju Institute of Science and Technology Korea 2 Department of Bio-Materials Graduate Schooland Research Center for Proteineous Materials Chosun University Gwangju Korea Keywords aggregation amphipathic helix antimicrobial peptides membrane depolarization proline Correspondence J. 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 9 February 2006 revised 28 June 2006 accepted 5 July 2006 doi Model amphipathic peptides have been widely used as a tool to determine the structural and biological properties that control the interaction of peptides with membranes. Here we have focused on the role of a central Pro in membrane-active peptides. To determine the role of Pro in structure antibiotic activity and interaction with phospholipids we generated a series of model amphipathic a-helical peptides with different chain lengths and containing or lacking a single central Pro. CD studies showed that Pro-free peptides PFPs formed stable a-helical structures even in aqueous buffer through self-association whereas Pro-containing peptides PCPs had random coil structures. In contrast in trifluoroethanol or SDS micelles both PFPs and PCPs adopted highly ordered a-helical structures although relatively lower helical contents were observed for the PCPs than the PFPs. This structural consequence indicates that a central Pro residue limits the formation of highly helical aggregates in aqueous buffer and causes a partial distortion of the stable a-helix in membrane-mimetic environments. With regard to antibiotic activity PCPs had a .

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