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Nisin adsorption on hydrophilic and hydrophobic surfaces: evidence of its interactions and antibacterial activity
Author(s) -
Karam Layal,
Jama Charafeddine,
Nuns Nicolas,
Mamede AnneSophie,
Dhulster Pascal,
Chihib NourEddine
Publication year - 2013
Publication title -
journal of peptide science
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.475
H-Index - 66
eISSN - 1099-1387
pISSN - 1075-2617
DOI - 10.1002/psc.2512
Subject(s) - adsorption , x ray photoelectron spectroscopy , nisin , chemistry , secondary ion mass spectrometry , substrate (aquarium) , hydrophobic effect , peptide , mass spectrometry , chemical engineering , protein adsorption , surface modification , combinatorial chemistry , polymer chemistry , organic chemistry , antimicrobial , chromatography , biochemistry , oceanography , engineering , geology
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 © 2013 European Peptide Society and John Wiley & Sons, Ltd.