caa a22 4500 397494564 CHVBK 20180308164518.0 cr unu---uuuuu 161202e199503 xx s 000 0 eng 10.1093/oxfordjournals.jbchem.a124744 doi (NATIONALLICENCE)oxford-10.1093/oxfordjournals.jbchem.a124744 Interaction of the Fragments Characteristic of Bactenecin 7 with Phospholipid Bilayers and Their Antimicrobial Activity [Elektronische Daten] [Ayako Tani, Sannamu Lee, Osamu Oishi, Haruhiko Aoyagi, Motonori Ohno] Bactenecin 7 (Bac7), a cationic polypeptide from large granules of bovine neutrophils, exhibits antimicrobial activity mainly against Gram-negative bacteria. This peptide is characterized by high contents of Arg and Pro and by a unique sequence with an Argclustered region and three tandem repeats. In order to investigate the structure-function relationship of Bac7, two peptide fragments, which correspond to residues 1-17 (RRIRPRPPRLPRPRPRP, an Arg-clustered region) and 46-59 (LPFPRPGPRPIPRP, one of three tandem repeats), respectively, were synthesized. Circular dichroism (CD) measurements of the two fragments indicated that they took particular conformations, although these were not denned. These peptides can bind to acidic phospholipid bilayers without marked conformational changes. When acidic phospholipid bilayers entrapping 5,6-carboxyfluorescein were treated with the peptides, no trace of the dye leaked out, indicating that the peptides lack the ability to disrupt lipid membranes. Fragment 1-17 showed weak antimicrobial activity against several bacteria, but fragment 46-59 was almost inactive. The present results suggest that longer fragments or the entire molecule of Bac7 may be required for full expression of antimicrobial activity and that Bac7 may manifest its activity by a bacteriostatic rather than a bacteriolytic mechanism. © 1995 BY THE JOURNAL OF BIOCHEMISTRY Regular Papers nationallicence antimicrobial activity nationallicence bactenecin 7 nationallicence cationic peptide nationallicence phospholipid bilayers nationallicence structure-function relationship nationallicence Tani Ayako Laboratory of Biochemistry, Department of Chemistry, Faculty of Science, Kyushu University Higashi-ku, Fukuoka, 812 aut Lee Sannamu Department of Chemistry, Faculty of Science, Fukuoka University Higashi-ku, Fukuoka 814-01 aut Oishi Osamu Laboratory of Biochemistry, Department of Chemistry, Faculty of Science, Kyushu University Higashi-ku, Fukuoka, 812 aut Aoyagi Haruhiko Department of Applied Chemistry, Faculty of Engineering, Nagasaki University Nagasaki, Nagasaki 852 aut Ohno Motonori Laboratory of Biochemistry, Department of Chemistry, Faculty of Science, Kyushu University Higashi-ku, Fukuoka, 812 aut The Journal of Biochemistry Oxford University Press 117/3(1995-03), 560-565 0021-924X 117:3<560 1995 117 jbchem https://doi.org/10.1093/oxfordjournals.jbchem.a124744 text/html Onlinezugriff via DOI 1 research-article jats NATIONALLICENCE 856 40 https://doi.org/10.1093/oxfordjournals.jbchem.a124744 text/html Onlinezugriff via DOI NATIONALLICENCE 700 1- Tani Ayako Laboratory of Biochemistry, Department of Chemistry, Faculty of Science, Kyushu University Higashi-ku, Fukuoka, 812 aut NATIONALLICENCE 700 1- Lee Sannamu Department of Chemistry, Faculty of Science, Fukuoka University Higashi-ku, Fukuoka 814-01 aut NATIONALLICENCE 700 1- Oishi Osamu Laboratory of Biochemistry, Department of Chemistry, Faculty of Science, Kyushu University Higashi-ku, Fukuoka, 812 aut NATIONALLICENCE 700 1- Aoyagi Haruhiko Department of Applied Chemistry, Faculty of Engineering, Nagasaki University Nagasaki, Nagasaki 852 aut NATIONALLICENCE 700 1- Ohno Motonori Laboratory of Biochemistry, Department of Chemistry, Faculty of Science, Kyushu University Higashi-ku, Fukuoka, 812 aut NATIONALLICENCE 773 0- The Journal of Biochemistry Oxford University Press 117/3(1995-03), 560-565 0021-924X 117:3<560 1995 117 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