Investigations of antimicrobial peptides in planar film systems

被引:53
作者
Volinsky, Roman
Kolusheva, Sofiya
Berman, Amir
Jefinek, Raz [1 ]
机构
[1] Ben Gurion Univ Negev, Dept Chem, IL-84103 Beer Sheva, Israel
[2] Ben Gurion Univ Negev, Dept Biotechnol Engn, IL-84103 Beer Sheva, Israel
[3] Ben Gurion Univ Negev, Ilse Katz Ctr Nanotechnol, IL-84103 Beer Sheva, Israel
来源
BIOCHIMICA ET BIOPHYSICA ACTA-BIOMEMBRANES | 2006年 / 1758卷 / 09期
关键词
Langmuir monolayer; Brewster angle microscopy; peptide-membrane interaction; peptide film;
D O I
10.1016/j.bbamem.2006.03.002
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
Planar systems - monolayers and films - constitute a useful platform for studying membrane-active peptides. Here, we summarize varied approaches for studying peptide organization and peptide-lipid interactions at the air/water interface, and focus on three representative antimicrobial membrane-associated peptides-alamethicin, gramicidin, and valinomycin. Experimental data, specifically surface pressure/area isotherms and Brewster angle microscopy images, provided information on peptide association and the effects of the lipid monolayers on peptide surface organization. In general, film analysis emphasized the effects of lipid layers in promoting peptide association and aggregation at the air/water interface. Importantly, the data demonstrated that in many cases peptide domains are phase-separated within the phospholipid monolayers, suggesting that this behavior contributes to the biological actions of membrane-active antimicrobial peptides. (c) 2006 Elsevier B.V. All rights reserved.
引用
收藏
页码:1393 / 1407
页数:15
相关论文
共 85 条
[1]   Conformation of alamethicin in oriented phospholipid bilayers determined by 15N solid-state nuclear magnetic resonance [J].
Bak, M ;
Bywater, RP ;
Hohwy, M ;
Thomsen, JK ;
Adelhorst, K ;
Jakobsen, HJ ;
Sorensen, OW ;
Nielsen, NC .
BIOPHYSICAL JOURNAL, 2001, 81 (03) :1684-1698
[2]   CONFORMATIONAL STUDY OF SEQUENTIAL LYS-BASED AND LEU-BASED POLYMERS AND OLIGOMERS USING VIBRATIONAL AND ELECTRONIC CD-SPECTRA [J].
BAUMRUK, V ;
HUO, DF ;
DUKOR, RK ;
KEIDERLING, TA ;
LELIEVRE, D ;
BRACK, A .
BIOPOLYMERS, 1994, 34 (08) :1115-1121
[3]   15N and 31P solid-state NMR investigations on the orientation of zervamicin II and alamethicin in phosphatidylcholine membranes [J].
Bechinger, B ;
Skladnev, DA ;
Ogrel, A ;
Li, X ;
Rogozhkina, EV ;
Ovchinnikova, TV ;
O'Neil, JDJ ;
Raap, J .
BIOCHEMISTRY, 2001, 40 (31) :9428-9437
[4]   Lipid-induced conformation and lipid-binding properties of cytolytic and antimicrobial peptides: determination and biological specificity [J].
Blondelle, SE ;
Lohner, K ;
Aguilar, MI .
BIOCHIMICA ET BIOPHYSICA ACTA-BIOMEMBRANES, 1999, 1462 (1-2) :89-108
[5]   Stability of an ion channel in lipid bilayers: Implicit solvent model calculations with gramicidin [J].
Bransburg-Zabary, S ;
Kessel, A ;
Gutman, M ;
Ben-Tal, N .
BIOCHEMISTRY, 2002, 41 (22) :6946-6954
[6]   First observation of mechanochromism at the nanometer scale [J].
Carpick, RW ;
Sasaki, DY ;
Burns, AR .
LANGMUIR, 2000, 16 (03) :1270-1278
[7]   CHROMISM IN POLYDIACETYLENE SOLUTIONS AND CRYSTALS [J].
CHANCE, RR .
MACROMOLECULES, 1980, 13 (02) :396-398
[8]   DIRECT COLORIMETRIC DETECTION OF A RECEPTOR-LIGAND INTERACTION BY A POLYMERIZED BILAYER ASSEMBLY [J].
CHARYCH, DH ;
NAGY, JO ;
SPEVAK, W ;
BEDNARSKI, MD .
SCIENCE, 1993, 261 (5121) :585-588
[9]   Distinguishing between different pathways of bilayer disruption by the related antimicrobial peptides cecropin B, B1 and B3 [J].
Chen, HM ;
Leung, KW ;
Thakur, NN ;
Tan, AM ;
Jack, RW .
EUROPEAN JOURNAL OF BIOCHEMISTRY, 2003, 270 (05) :911-920
[10]   Polymyxin B-lipid interactions in Langmuir-Blodgett monolayers of Escherichia coli lipids:: A thermodynamic and atomic force microscopy study [J].
Clausell, A ;
Busquets, MA ;
Pujol, M ;
Alsina, A ;
Cajal, Y .
BIOPOLYMERS, 2004, 75 (06) :480-490