Ghang Yoo-Jin, Perez Lizeth, Morgan Melissa A, Si Fang, Hamdy Omar M, Beecher Consuelo N, Larive Cynthia K, Julian Ryan R, Zhong Wenwan, Cheng Quan, Hooley Richard J
University of California - Riverside, Department of Chemistry, Riverside, CA 92521, USA.
Soft Matter. 2014 Dec 28;10(48):9651-6. doi: 10.1039/c4sm02347a. Epub 2014 Nov 4.
An anionic self-folding deep cavitand is capable of immobilizing unmodified proteins and enzymes at a supported lipid bilayer interface, providing a simple, soft bioreactive surface that allows enzymatic function under mild conditions. The adhesion is based on complementary charge interactions, and the hosts are capable of binding enzymes such as trypsin at the bilayer interface: the catalytic activity is retained upon adhesion, allowing selective reactions to be performed at the membrane surface.
一种阴离子自折叠深穴配体能够将未修饰的蛋白质和酶固定在支撑脂质双层界面上，提供一个简单、柔软的生物反应表面，使酶在温和条件下发挥功能。这种吸附作用基于互补电荷相互作用，这些主体能够在双层界面结合诸如胰蛋白酶等酶：吸附后酶的催化活性得以保留，从而能够在膜表面进行选择性反应。
