将脲酶特异性定位于 DNA 折纸并使其具有持续活性的方法

Ian Murphy, Keren Bobilev, Daichi Hayakawa, Eden Ikonen, Thomas E. Videbæk, Shibani Dalal, Wylie W. Ahmed, Jennifer L. Ross, W. Benjamin Rogers
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引用次数: 0

摘要

将酶连接到纳米结构已被证明有助于在受控条件下研究酶的功能,并催生了新技术。通常情况下,酶系纳米结构的实用性和趣味性在于酶的活性如何受到酶在空间排列方式的影响。在本文中,我们介绍了一种在保持酶活性的同时将单链 DNA 与脲酶共轭的方法。我们展示了成功共轭的证据,并量化了影响共轭产量的变量。最后,我们展示了利用 DNA 折纸技术将脲酶系在纳米结构上,而且具有高度的位点特异性。用具有酶活性的脲酶装饰纳米结构可能会有助于研究甚至利用脲酶在从生物技术到软物质物理学等学科中的功能。我们在本文中介绍的技术将使这些领域的研究人员能够在不破坏酶功能的情况下改造酶,从而对酶的行为和用途进行更深入的研究。
本文章由计算机程序翻译,如有差异,请以英文原文为准。
A method for site-specifically tethering the enzyme urease to DNA origami with sustained activity
Attaching enzymes to nanostructures has proven useful to the study of enzyme functionality under controlled conditions and has led to new technologies. Often, the utility and interest of enzyme-tethered nanostructures lie in how the enzymatic activity is affected by how the enzymes are arranged in space. Therefore, being able to conjugate enzymes to nanostructures while preserving the enzymatic activity is essential. In this paper, we present a method to conjugate single-stranded DNA to the enzyme urease while maintaining enzymatic activity. We show evidence of successful conjugation and quantify the variables that affect the conjugation yield. We also show that the enzymatic activity is unchanged after conjugation compared to the enzyme in its native state. Finally, we demonstrate the tethering of urease to nanostructures made using DNA origami with high site-specificity. Decorating nanostructures with enzymatically-active urease may prove to be useful in studying, or even utilizing, the functionality of urease in disciplines ranging from biotechnology to soft-matter physics. The techniques we present in this paper will enable researchers across these fields to modify enzymes without disrupting their functionality, thus allowing for more insightful studies into their behavior and utility.
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