Murphy Ian, Bobilev Keren, Hayakawa Daichi, Ikonen Eden, Videbæk Thomas E, Dalal Shibani, Ahmed Wylie W, Ross Jennifer L, Rogers W Benjamin
Martin A. Fisher School of Physics, Brandeis University, Waltham, Massachusetts, United States of America.
Laboratoire de Physique Théorique (LPT), Université de Toulouse, CNRS, UPS, Toulouse, France.
PLoS One. 2025 Apr 21;20(4):e0319790. doi: 10.1371/journal.pone.0319790. eCollection 2025.
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.
将酶附着于纳米结构已被证明对在可控条件下研究酶的功能很有用,并催生了新技术。通常,酶系纳米结构的实用性和吸引力在于酶的空间排列方式如何影响酶活性。因此,能够在保持酶活性的同时将酶与纳米结构偶联至关重要。在本文中,我们提出了一种在保持酶活性的同时将单链DNA与脲酶偶联的方法。我们展示了成功偶联的证据,并对影响偶联产率的变量进行了量化。我们还表明,与天然状态的酶相比,偶联后酶活性未发生变化。最后,我们证明了脲酶以高位点特异性连接到使用DNA折纸术制备的纳米结构上。用具有酶活性的脲酶修饰纳米结构可能在从生物技术到软物质物理学等学科中研究甚至利用脲酶的功能方面很有用。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对酶进行修饰,从而更深入地研究其行为和用途。