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- W338575478 abstract "The protein binding capability of biomaterial surfaces can significantly affect subsequent biological responses, and appropriate ligand presentation is often required to guarantee the best functions. Herein, a new facile method for regulating this capability by varying the localized and average ligand density is presented. Binding between lysine and plasminogen relevant to a fibrinolysis system was chosen as a model. We integrated different lysine-modified β-cyclodextrin (β-CD) derivatives onto bioinert copolymer brushes via host–guest interactions. The localized and average lysine density can be conveniently modulated by changing the lysine valency on β-CD scaffolds and by diluting lysine-persubstituted β-CD with pure β-CD, respectively. Both the plasminogen adsorption and the plasminogen binding affinity were enhanced by lysine-persubstituted β-CD compared with those of lysine-monosubstituted β-CD, which is possibly due to the higher localized lysine density and the multivalent binding of plasminogen on lysine-persubstituted β-CD surfaces. With a change in the ratio of lysine-persubstituted β-CD to β-CD, the average lysine density can be tuned, leading to the linear regulation of the adsorption of plasminogen on surfaces." @default.
- W338575478 created "2016-06-24" @default.
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- W338575478 date "2015-05-22" @default.
- W338575478 modified "2023-10-16" @default.
- W338575478 title "Regulation of Protein Binding Capability of Surfaces via Host–Guest Interactions: Effects of Localized and Average Ligand Density" @default.
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- W338575478 doi "https://doi.org/10.1021/acs.langmuir.5b01380" @default.
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