caa a22 4500 397555733 CHVBK 20180308164801.0 cr unu---uuuuu 161202e199612 xx s 000 0 eng 10.1093/oxfordjournals.jbchem.a021532 doi (NATIONALLICENCE)oxford-10.1093/oxfordjournals.jbchem.a021532 Selective Interaction of Synthetic Antimicrobial Peptides Derived from Sapecin B with Lipid Bilayers [Elektronische Daten] [Yutaka Hirakura, Juan Alverez-Bravo, Sho-ichiro Kurata, Shunji Natori, Yutaka Kirino] By measuring carboxyfluorescein leakage from liposomes and the increase in membrane current through planar lipid bilayer membranes, we examined the capacities of a series of low-molecular-weight cationic ainphiphilic peptides derived from the α-helix domain of sapecin B for membrane-perturbation and ion-channel formation. Some of these peptides strongly interact with membranes containing acidic phospholipids and phosphatidylethanolamine, with a very negative potential, which are characteristic of the Escherichia coli membrane, in parallel with their antimicrobial activity. In contrast, they do not interact with membranes which predominantly contain choline phospholipids and cholesterol in their outer leaflets, with a slightly negative potential, all of which are characteristic of eukaryotic membranes, thereby providing a molecular basis for their selective toxicity. Membranes doped with these peptides are as permeable to inorganic phosphates as to chloride ions and are far more permeable to cations. The loss of inorganic phosphates may damage bacterial cells due to rapid depletion of cytoplasmic ATP. Examination of the structure-activity relationships of a series of derived peptides in their interaction with a model of the E. coli membrane confirmed the necessity of cationic amphiphilicity for the peptides to attack the bacterial membrane and to exhibit antimicrobial activity. © 1996 BY THE JOURNAL OF BIOCHEMISTRY Regular Papers nationallicence amphiphilicity nationallicence antimirobial peptide nationallicence liposome nationallicence planer bilayer nationallicence selective toxicity nationallicence Hirakura Yutaka Faculty of Pharmaceutical Sciences, The University of Tokyo, Hong, Bunkyo-ku, Tokyo 113 aut Alverez-Bravo Juan Faculty of Pharmaceutical Sciences, The University of Tokyo, Hong, Bunkyo-ku, Tokyo 113 aut Kurata Sho-ichiro Faculty of Pharmaceutical Sciences, The University of Tokyo, Hong, Bunkyo-ku, Tokyo 113 aut Natori Shunji Faculty of Pharmaceutical Sciences, The University of Tokyo, Hong, Bunkyo-ku, Tokyo 113 aut Kirino Yutaka Faculty of Pharmaceutical Sciences, The University of Tokyo, Hong, Bunkyo-ku, Tokyo 113 aut The Journal of Biochemistry Oxford University Press 120/6(1996-12), 1130-1140 0021-924X 120:6<1130 1996 120 jbchem https://doi.org/10.1093/oxfordjournals.jbchem.a021532 text/html Onlinezugriff via DOI 1 other jats NATIONALLICENCE 856 40 https://doi.org/10.1093/oxfordjournals.jbchem.a021532 text/html Onlinezugriff via DOI NATIONALLICENCE 700 1- Hirakura Yutaka Faculty of Pharmaceutical Sciences, The University of Tokyo, Hong, Bunkyo-ku, Tokyo 113 aut NATIONALLICENCE 700 1- Alverez-Bravo Juan Faculty of Pharmaceutical Sciences, The University of Tokyo, Hong, Bunkyo-ku, Tokyo 113 aut NATIONALLICENCE 700 1- Kurata Sho-ichiro Faculty of Pharmaceutical Sciences, The University of Tokyo, Hong, Bunkyo-ku, Tokyo 113 aut NATIONALLICENCE 700 1- Natori Shunji Faculty of Pharmaceutical Sciences, The University of Tokyo, Hong, Bunkyo-ku, Tokyo 113 aut NATIONALLICENCE 700 1- Kirino Yutaka Faculty of Pharmaceutical Sciences, The University of Tokyo, Hong, Bunkyo-ku, Tokyo 113 aut NATIONALLICENCE 773 0- The Journal of Biochemistry Oxford University Press 120/6(1996-12), 1130-1140 0021-924X 120:6<1130 1996 120 jbchem Metadata rights reserved CC BY-NC-4.0 http://creativecommons.org/licenses/by-nc/4.0 nationallicence BK010053 XK010053 XK010000 NATIONALLICENCE NATIONALLICENCE NL-oxford