Deshapriya I K, Kumar C V
Department of Chemistry, University of Connecticut, Storrs, Connecticut, USA.
Department of Chemistry, University of Connecticut, Storrs, Connecticut, USA; Department of Molecular and Cell Biology, University of Connecticut, Storrs, Connecticut, USA; Institute of Material Science, University of Connecticut, Storrs, Connecticut, USA; Department of Inorganic and Physical Chemistry, Indian Institute of Science, Bengaluru, Karnataka, India.
Methods Enzymol. 2016;571:151-75. doi: 10.1016/bs.mie.2016.02.006. Epub 2016 Mar 30.
Rational approaches for the control of nano-bio interfaces for enzyme stabilization are vital for engineering advanced, functional nanobiocatalysts, biosensors, implants, or "smart" drug delivery systems. This chapter presents an overview of our recent efforts on structural, functional, and mechanistic details of enzyme nanomaterials design, and describes how progress is being made by hypothesis-driven rational approaches. Interactions of a number of enzymes having wide ranges of surface charges, sizes, and functional groups with α-Zr(IV)phosphate (α-ZrP) nanosheets are carefully controlled to achieve high enzyme binding affinities, excellent loadings, significant retention of the bound enzyme structure, and high enzymatic activities. In specific cases, catalytic activities and selectivities of the nanobiocatalysts are improved over those of the corresponding pristine enzymes. Maximal enzyme structure retention has been obtained by coating the nanosheets with appropriate proteinaceous materials to soften the enzyme-nanosheet interface. These systematic manipulations are of significant importance to understand the complex behavior of enzymes at inorganic surfaces.
合理控制纳米生物界面以实现酶的稳定化,对于构建先进的功能性纳米生物催化剂、生物传感器、植入物或“智能”药物递送系统至关重要。本章概述了我们近期在酶纳米材料设计的结构、功能和机理细节方面所做的努力,并描述了如何通过假设驱动的合理方法取得进展。仔细控制多种具有广泛表面电荷、大小和官能团的酶与α-磷酸锆(α-ZrP)纳米片之间的相互作用,以实现高酶结合亲和力、优异的负载量、结合酶结构的显著保留以及高酶活性。在特定情况下,纳米生物催化剂的催化活性和选择性比相应的原始酶有所提高。通过用适当的蛋白质材料包覆纳米片以软化酶-纳米片界面,已实现了最大程度的酶结构保留。这些系统性操作对于理解酶在无机表面的复杂行为具有重要意义。