Evaluation of Enzymatic Activity on Nanoscale Polystyrene-block-Polymethylmethacrylate Diblock Copolymer Domains

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• 作者：Omkar Parajuli ; Abhishek Gupta ; Nitin Kumar ; Jong-in Hahm
• 刊名：Journal of Physical Chemistry B
• 出版年：2007
• 出版时间：December 20, 2007
• 年：2007
• 卷：111
• 期：50
• 页码：14022 - 14027
• 全文大小：438K
• 年卷期：v.111,no.50(December 20, 2007)
• ISSN：1520-5207

文摘

Understanding structural and functional changes of polymeric surface-bound proteins is extremely importantas polymers play an increasingly significant role as arrays and substrates in proteomics applications. Wecarried out, for the first time, quantitative activity measurements of horseradish peroxidase (HRP) enzymesimmobilized selectively on the polystyrene domains of microphase-separated polystyrene-block-polymethylmethacrylate ultrathin films. The specific enzymatic activity of HRP adsorbed on the diblock copolymersurface was evaluated and compared to that of HRP in free solution. We demonstrate that the polymericsurface-bound HRP molecules maintain approximately 85% of their activity in free solution. The uniqueadvantages of diblock copolymer templates, involving nanoscale self-assembly and largely retained proteinfunctionality, make the spontaneously constructed enzyme nanoarrays highly suitable as proteomics substrates.Our novel assembly method of providing functional enzymes on diblock copolymer thin films can be greatlybeneficial for high-throughput and high-density protein assays.