Zheng Haifu, Du Xuezhong
Key Laboratory of Mesoscopic Chemistry (Ministry of Education), School of Chemistry and Chemical Engineering, Nanjing University, Nanjing 210093, People's Republic of China.
J Phys Chem B. 2009 Aug 13;113(32):11330-7. doi: 10.1021/jp9060279.
Concanavalin A (Con A) binding to the surfaces of mannose-functionalized binary monolayers was enhanced by surface molecular imprinting technique. The protein surface imprinting was prepared from binary Langmuir monolayers at the air-water interface through lateral reorganization of glycolipids directed by Con A in the subphase solution to form more specific bivalent binding sites, followed by horizontal immobilization of the binary monolayers and preservation of the enhanced affinity. The favorable spatial arrangement of the mannose ligands through lateral delivery matched well with protein binding pockets, and the steric crowding/hindrance of neighboring ligands was minimized. The amounts of specifically bound proteins on the imprint surfaces are almost independent of surface density of the ligands, in contrast to the dependence of the bound amounts on surface density of the ligands for the control surfaces. The benefits of the protein surface imprinting included excellent mass transfer, ease of integration into sensor systems, directed creation of imprint sites, and biologically friendly aqueous media. This strategy generated tailor-made surfaces with high protein affinity and opens the possibility of surface design of intellectual materials and preparation of biosensors.
通过表面分子印迹技术增强了伴刀豆球蛋白A（Con A）与甘露糖功能化二元单层表面的结合。蛋白质表面印迹是在气-水界面由二元朗缪尔单层通过亚相溶液中Con A引导的糖脂横向重组制备而成，以形成更具特异性的二价结合位点，随后将二元单层水平固定并保留增强的亲和力。通过横向递送使甘露糖配体形成有利的空间排列，与蛋白质结合口袋匹配良好，且相邻配体的空间拥挤/位阻最小化。与对照表面上结合量对配体表面密度的依赖性相反，印迹表面上特异性结合的蛋白质数量几乎与配体的表面密度无关。蛋白质表面印迹的优点包括出色的传质性能、易于集成到传感器系统、定向创建印迹位点以及生物友好的水性介质。该策略产生了具有高蛋白质亲和力的定制表面，并为智能材料的表面设计和生物传感器的制备开辟了可能性。
