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• W2323984886 endingPage "15091" @default.
• W2323984886 startingPage "15083" @default.
• W2323984886 abstract "Patchy polymer brushes contain nanoscale (5–15 nm) adhesive elements, such as polymer coils or nanoparticles, embedded at their base at random positions on the surface. The competition between the brush’s steric (protein resistant) repulsions and the attractions from the discrete adhesive elements provides a precise means to control bioadhesion. This differs from the classical approach, where functionality is placed on the brush’s periphery. The current study demonstrates the impact of poly(etheylene glycol) (PEG) brush architecture and ionic strength on fibrinogen adsorption on brushes containing embedded poly-l-lysine (PLL, 20K MW) coils or “patches”. The consistent appearance of a fibrinogen adsorption threshold, a minimum loading of patches on the surface, below which protein adsorption does not occur, suggests multivalent protein capture: Adsorbing proteins simultaneously engage several patches. The surface composition (patch loading) at the threshold is extremely sensitive to the brush height and ionic strength, varying up to a factor of 5 in the surface loading of the PLL patches (∼50% of the range of possible surfaces). Variations in ionic strength have a similar effect, with the smallest thresholds seen for the largest Debye lengths. While trends with brush height were the clearest and most dominant, consideration of the PEG loading within the brush or its persistence length did not reveal a critical brush parameter for the onset of adsorption. The lack of straightforward correlation on brush physics was likely a result of multivalent binding, (producing an additional dependence on patch loading), and might be resolved for univalent adsorption onto more strongly binding patches. While studies with similar brushes placed uniformly on a surface revealed that the PEG loading within the brush is the best indicator of protein resistance, the current results suggest that brush height is more important for patchy brushes. Likely the interactions producing brush extension normal to the interface act similarly to drive lateral tether extension to obstruct patches." @default.
• W2323984886 created "2016-06-24" @default.
• W2323984886 creator A5017673921 @default.
• W2323984886 creator A5042356436 @default.
• W2323984886 date "2011-11-21" @default.
• W2323984886 modified "2023-09-26" @default.
• W2323984886 title "Sensitivity of Protein Adsorption to Architectural Variations in a Protein-Resistant Polymer Brush Containing Engineered Nanoscale Adhesive Sites" @default.
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• W2323984886 doi "https://doi.org/10.1021/la203293k" @default.
• W2323984886 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/22040182" @default.
• W2323984886 hasPublicationYear "2011" @default.
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