Interfacial Conformation of Hydrophilic Polyphosphoesters Affects Blood Protein Adsorption

Christoph Bernhard, Kristin N. Bauer, Mischa Bonn, Frederik R. Wurm, Grazia Gonella*

*Corresponding author for this work

Research output: Contribution to journalArticleAcademicpeer-review

10 Citations (Scopus)

Abstract

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.1624-1629
Original languageEnglish
Pages (from-to)1624-1629
JournalACS applied materials & interfaces
Volume11
Issue number1
DOIs
Publication statusPublished - 9 Jan 2019
Externally publishedYes

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