The affinity of two antimicrobial peptides derived from bovine milk proteins for model lipid membranes

被引：21

作者：

Barzyk, Wanda ^{[2
]}

Campagna, Sylvie ^{[3
]}

Wieclaw, Katarzyna ^{[1
,4
]}

Korchowiec, Beata ^{[1
,4
]}

Rogalska, Ewa ^{[1
]}

机构：

[1] Nancy Univ, CNRS, F-54506 Vandoeuvre Les Nancy, France

[2] Polish Acad Sci, Inst Catalysis & Surface Chem, PL-30239 Krakow, Poland

[3] Nancy Univ, INRA, URAFPA, Equipe Proteolyse Biofonct Prot & Peptides, F-54506 Vandoeuvre Les Nancy, France

[4] Jagiellonian Univ, Fac Chem, Dept Phys Chem & Electrochem, PL-30060 Krakow, Poland

来源：

COLLOIDS AND SURFACES A-PHYSICOCHEMICAL AND ENGINEERING ASPECTS | 2009年 / 343卷 / 1-3期

关键词：

1,2-Dipalmitoyl-sn-glycero-3-phosphocholine; 1,2-Dipalmitoyl-sn-glycero-3-phospho-rac-(1-glycerol); Peptide-membrane interactions; Langmuir films; Phospholipid monolayers; MONOLAYERS; COMPONENT; PP3;

D O I：

10.1016/j.colsurfa.2009.01.036

中图分类号：

O64 [物理化学（理论化学）、化学物理学];

学科分类号：

070305 [高分子化学与物理];

摘要：

In this work, two antimicrobial peptides were studied regarding their capacity to interact with lipid membranes. The peptides subsequently named L-16-Y and N-23-T were derived from the bovine milk alpha-s2 casein and from the component-3 of proteose peptone (PP3), respectively. 1,2-Dipalmitoylsn-glycero-3-phosphocholine (DPPG) and 1,2-dipalmitoyl-sn-glycero-3-phospho-rac-(1-glycerol) (DPPC) monomolecular films spread at the air-water interface were used, respectively, as model host and bacterial membranes. The surface pressure and surface potential measurements, as well as Brewster angle microscopy (BAM) showed that both peptides interact with the model membranes. However, the higher affinity for DPPG compared to DPPC indicates that these peptides are innocuous for the host membranes. (C) 2009 Elsevier B.V. All rights reserved.

引用

页码：104 / 110

页数：7

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