Nisin adsorption on hydrophilic and hydrophobic surfaces: evidence of its interactions and antibacterial activity

被引:32
作者
Karam, Layal [1 ,2 ]
Jama, Charafeddine [2 ]
Nuns, Nicolas [3 ]
Mamede, Anne-Sophie [3 ]
Dhulster, Pascal [1 ]
Chihib, Nour-Eddine [1 ]
机构
[1] Univ Lille 1, Polytech Lille, Lab ProBioGEM, F-59655 Villeneuve Dascq, France
[2] Univ Lille 1, Ecole Natl Super Chim Lille, CNRS, Lab UMET,UMR 8207, F-59655 Villeneuve Dascq, France
[3] Univ Lille 1, Ecole Natl Super Chim Lille, CNRS, Unite Catalyse & Chim Solide,UMR 8181, F-59655 Villeneuve Dascq, France
关键词
peptides adsorption; peptides interactions; antimicrobial surfaces; nisin; peptides characterization; hydrophobic surfaces; hydrophilic surfaces; materials' interfaces; X-ray photoelectron spectroscopy (XPS); time-of-flight secondary ion mass spectrometry (ToF-SIMS); PROTEIN ANTIMICROBIAL BARRIERS; BACTERIAL ADHESION; TOF-SIMS;
D O I
10.1002/psc.2512
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
Study of peptides adsorption on surfaces remains a current challenge in literature. A complementary approach, combining X-ray photoelectron spectroscopy (XPS) and time-of-flight secondary ion mass spectrometry (ToF-SIMS) was used to investigate the antimicrobial peptide nisin adsorption on hydrophilic and hydrophobic surfaces. The native low density polyethylene was used as hydrophobic support and it was grafted with acrylic acid to render it hydrophilic. XPS permitted to confirm nisin adsorption and to determine its amount on the surfaces. ToF-SIMS permitted to identify the adsorbed bacteriocin type and to observe its distribution and orientation behavior on both types of surfaces. Nisin was more oriented by its hydrophobic side to the hydrophobic substrate and by its hydrophilic side to the outer layers of the adsorbed peptide, in contrast to what was observed on the hydrophilic substrate. A correlation was found between XPS and ToF-SIMS results, the types of interactions on both surfaces and the observed antibacterial activity. Such interfacial studies are crucial for better understanding the peptides interactions and adsorption on surfaces and must be considered when setting up antimicrobial surfaces. Copyright (c) 2013 European Peptide Society and John Wiley & Sons, Ltd.
引用
收藏
页码:377 / 385
页数:9
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