Morphological Changes Induced by the Action of Antimicrobial Peptides on Supported Lipid Bilayers

被引:32
作者
Arouri, Ahmad [1 ]
Kiessling, Volker [2 ]
Tamm, Lukas [2 ]
Dathe, Margitta [3 ]
Blume, Alfred [1 ]
机构
[1] Univ Halle Wittenberg, Inst Chem, D-06120 Halle, Germany
[2] Univ Virginia, Dept Mol Physiol & Biol Phys, Charlottesville, VA USA
[3] Inst Mol Pharmacol, D-13125 Berlin, Germany
关键词
INTERFERENCE-CONTRAST MICROSCOPY; AMPHIPATHIC MODEL PEPTIDES; PORE-FORMING PEPTIDE; PHOSPHOLIPID-BILAYERS; TRYPTOPHAN-RICH; PLANAR BILAYERS; ARGININE-RICH; MEMBRANES; MONOLAYERS; VESICLES;
D O I
10.1021/jp107577k
中图分类号
O64 [物理化学(理论化学)、化学物理学];
学科分类号
070304 ; 081704 ;
摘要
We utilized epifluorescence microscopy to investigate the morphological changes in labeled lipid bilayers supported on quartz surfaces (SLBs) induced by the interaction of cationic antimicrobial peptides with the lipid membranes. The SLBs were prepared from 1-palmitoyl-2-oleoyl-sn-glycero-3-phosphoglycerol (POPG), 1-palmitoyl-2-oleoyl-sn-glycero-3-phosphocholine (POPC), 1-palmitoyl-2-oleoyl-sn-glycero-3-phosphoethanolamine (POPE) and mixtures thereof as well as from Escherichia con lipid extract. We succeeded in the preparation of POPG and POPG-rich SLBs without the necessity to use fusogenic agents such as calcium by using the Langmuir-Blodgett/Langmuir-Schaefer transfer method. The adsorption of the peptides to the SLBs was initially driven by electrostatic interactions with the PG headgroups and led to the formation of lipid protrusions bulging out from the lipid layer facing the bulk, originating particularly from domain boundaries and membrane defects. The shape, size, and frequency of the lipid protrusions are mainly controlled by the peptide macroscopic properties and the membrane composition. A restructuring of the lipid protrusions into other structures can also occur over time.
引用
收藏
页码:158 / 167
页数:10
相关论文
共 66 条
[41]   DIVALENT-CATION INDUCED FUSION AND LIPID LATERAL SEGREGATION IN PHOSPHATIDYLCHOLINE PHOSPHATIDIC-ACID VESICLES [J].
LEVENTIS, R ;
GAGNE, J ;
FULLER, N ;
RAND, RP ;
SILVIUS, JR .
BIOCHEMISTRY, 1986, 25 (22) :6978-6987
[42]   Differential scanning microcalorimetry indicates that human defensin, HNP-2, interacts specifically with biomembrane mimetic systems [J].
Lohner, K ;
Latal, A ;
Lehrer, RI ;
Ganz, T .
BIOCHEMISTRY, 1997, 36 (06) :1525-1531
[43]  
Lohner K, 2008, ADV PLANAR LIP BILAY, V6, P103, DOI 10.1016/S1554-4516(07)06005-X
[44]   Real-time monitoring of melittin-induced pore and tubule formation from supported lipid bilayers and its physiological relevance [J].
Machan, Radek ;
Miszta, Adam ;
Hermens, Wim ;
Hof, Martin .
CHEMISTRY AND PHYSICS OF LIPIDS, 2010, 163 (02) :200-206
[45]   The response of giant phospholipid vesicles to pore-forming peptide melittin [J].
Mally, Mojca ;
Majhenc, Janja ;
Svetina, Sasa ;
Zeks, Bostjan .
BIOCHIMICA ET BIOPHYSICA ACTA-BIOMEMBRANES, 2007, 1768 (05) :1179-1189
[46]   Composition dependence of vesicle morphology and mixing properties in a bacterial model membrane system [J].
Navas, BP ;
Lohner, K ;
Deutsch, G ;
Sevcsik, S ;
Riske, KA ;
Dimova, R ;
Garidel, P ;
Pabst, G .
BIOCHIMICA ET BIOPHYSICA ACTA-BIOMEMBRANES, 2005, 1716 (01) :40-48
[47]   LIPID VESICLE ADSORPTION VERSUS FORMATION OF PLANAR BILAYERS ON SOLID-SURFACES [J].
NOLLERT, P ;
KIEFER, H ;
JAHNIG, F .
BIOPHYSICAL JOURNAL, 1995, 69 (04) :1447-1455
[48]   DIVALENT CATION-INDUCED PHOSPHATIDIC-ACID MEMBRANE-FUSION - EFFECT OF ION BINDING AND MEMBRANE-SURFACE TENSION [J].
OHKI, S ;
OHSHIMA, H .
BIOCHIMICA ET BIOPHYSICA ACTA, 1985, 812 (01) :147-154
[50]   Peptide-Induced Domain Formation in Supported Lipid Bilayers: Direct Evidence by Combined Atomic Force and Polarized Total Internal Reflection Fluorescence Microscopy [J].
Oreopoulos, John ;
Epand, Raquel F. ;
Epand, Richard M. ;
Yip, Christopher M. .
BIOPHYSICAL JOURNAL, 2010, 98 (05) :815-823