Journal
ACS APPLIED MATERIALS & INTERFACES
Volume 11, Issue 1, Pages 1624-1629Publisher
AMER CHEMICAL SOC
DOI: 10.1021/acsami.8b17146
Keywords
nonfouling polymer coatings; hydrophilic polymers; conformation; steric hindrance; hydration
Funding
- Max Planck Graduate Center
- Johannes Gutenberg University Mainz through a PhD fellowship
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Synthetic polymers are commonly used as protein repelling materials for a variety of biomedical applications. Despite their widespread use, the fundamental mechanism underlying protein repellence is often elusive. Such insights are essential for improving existing and developing new materials. Here, we investigate how subtle differences in the chemistry of hydrophilic polyphosphoesters influence the adsorption of the human blood proteins serum albumin and fibrinogen. Using thermodynamic measurements, surface-specific vibrational spectroscopy, and Brewster angle microscopy, we investigate protein adsorption, hydration, and steric repulsion properties of the polyphosphoester polymers. Whereas both surface hydration and polymer conformation of the polymers vary substantially as a consequence of the chemical differences in the polymer structure, the protein repellency ability of these hydrophilic materials appears to be dominated by steric repulsion.
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