Drastically Lowered Protein Adsorption on Microbicidal Hydrophobic/Hydrophilic Polyelectrolyte Multilayers

Polyelectrolyte multilayer films assembled from a hydrophobic N-alkylated polyethylenimine and a hydrophilic polyacrylate were discovered to exhibit strong antifouling, as well as antimicrobial, activities. Surfaces coated with these layer-by-layer (LbL) films, which range from 6 to 10 bilayers (up...

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Bibliographic Details
Published in:Biomacromolecules 2012-03, Vol.13 (3), p.719-726
Main Authors: Wong, Sze Yinn, Han, Lin, Timachova, Ksenia, Veselinovic, Jovana, Hyder, Md Nasim, Ortiz, Christine, Klibanov, Alexander M, Hammond, Paula T
Format: Article
Language:English
Subjects:
Animals
Anti-Bacterial Agents - chemistry
Anti-Bacterial Agents - pharmacology
Applied sciences
Biofouling - prevention & control
Biological properties
Blood Proteins - chemistry
Blood Proteins - metabolism
Cattle
Cell Adhesion - drug effects
Electrolytes - chemistry
Exact sciences and technology
Hydrophobic and Hydrophilic Interactions
Microscopy, Atomic Force
Microscopy, Electron, Scanning
Organic polymers
Physicochemistry of polymers
Polymers - chemistry
Polymers - pharmacology
Properties and characterization
Surface Properties
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Summary:Polyelectrolyte multilayer films assembled from a hydrophobic N-alkylated polyethylenimine and a hydrophilic polyacrylate were discovered to exhibit strong antifouling, as well as antimicrobial, activities. Surfaces coated with these layer-by-layer (LbL) films, which range from 6 to 10 bilayers (up to 45 nm in thickness), adsorbed up to 20 times less protein from blood plasma than the uncoated controls. The dependence of the antifouling activity on the nature of the polycation, as well as on assembly conditions and the number of layers in the LbL films, was investigated. Changing the hydrophobicity of the polycation altered the surface composition and the resistance to protein adsorption of the LbL films. Importantly, this resistance was greater for coated surfaces with the polyanion on top; for these films, the average zeta potential pointed to a near neutral surface charge, thus, presumably minimizing their electrostatic interactions with the protein. The film surface exhibited a large contact angle hysteresis, indicating a heterogeneous topology likely due to the existence of hydrophobic–hydrophilic regions on the surface. Scanning electron micrographs of the film surface revealed the existence of nanoscale domains. We hypothesize that the existence of hydrophobic/hydrophilic nanodomains, as well as surface charge neutrality, contributes to the LbL film’s resistance to protein adsorption.
ISSN:1525-7797
1526-4602
DOI:10.1021/bm201637e