Polymeric vesicles mimicking glycocalyx (PV-Gx) for studying carbohydrate–protein interactions in solution
Polymeric vesicles mimicking glycocalyx (PV-Gx) for studying carbohydrate–protein interactions in solution
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DOI：
10.1039/c2py20110k
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发表时间：
2012-05
影响因子：
4.6
通讯作者：
Lu Su;Yu Zhao;Guosong Chen;Ming Jiang
中科院分区：
文献类型：
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作者：
Lu Su;Yu Zhao;Guosong Chen;Ming Jiang
糖萼是细胞表面的碳水化合物外壳，已被证明在各种生物事件中特别重要。在这项工作中，聚合物囊泡模拟的糖萼（PV-Gx），作为一个简化的模型系统，是通过我们的NCCM（非共价连接胶束）的策略。简单地说，通过RAFT聚合制备了具有苯基硼酸（BA）末端的热响应性聚（N-异丙基丙烯酰胺）（BA-PNIPAM）和两种新型亲水性糖基共聚物PGal和PGlc，其中PGlc是由分别含有半乳糖苷（Gal）和葡萄糖苷（Glc）单元的N-连接的β-吡喃糖苷单体制备的。在加热时，PNIPAM-BA和PGal（PGlc）通过糖和BA之间的动态共价键驱动自组装成囊泡V-PGal（V-PGlc）。V-PGal和V-PGlc都可以作为我们的目标人工糖萼（PV-Gx），因为它们具有糖包被的表面和在水中稳定分散。动态光散射（DLS）已被用于监测PV-Gx上的糖与三种凝集素即花生（PNA）、鸡冠刺桐（ECA）和伴刀豆球蛋白A（Con A）之间的结合过程，结论是PV-Gx在糖-蛋白相互作用中显示出明显的特异性：V-PGal与PNA和ECA很好地相互作用以形成聚集体，但不与ConA相互作用，而V-PGlc不与凝集素相互作用。结果清楚地证明，由具有明确定义的糖单元的聚合物构建的PV-Gx是一个新的和有前途的平台，用于研究溶液中的碳水化合物-蛋白质相互作用。
Glycocalyx, the carbohydrate coat on cell surfaces, has been proved to be particularly important in a variety of biological events. In this work, polymeric vesicle mimicking of glycocalyx (PV-Gx), as a simplified model system, is achieved via our NCCM (non-covalently connected micelles) strategy. Briefly, a thermal responsive poly(N-isopropylacrylamide) with phenylboronic acid (BA) end (BA-PNIPAM) and two novel hydrophilic glycopolymers, PGal and PGlc are prepared by RAFT polymerization, where the latter are prepared from N-linked β-pyranoside monomers containing respective units of galactoside (Gal) and glucoside (Glc). Upon heating PNIPAM-BA and PGal (PGlc) self-assemble into vesicles V-PGal (V-PGlc), driven by the dynamic covalent bond between sugars and BA. Both V-PGal and V-PGlc could serve as our target artificial glycocalyx (PV-Gx) because they have sugar-coated surfaces and disperse stably in water. Dynamic light scattering (DLS) has been employed to monitor the binding process between the sugars on PV-Gx and three lectins i.e. Arachis hypogaea (PNA), Erythrina cristagalli (ECA) and Concanavalin A (Con A), concluding that the PV-Gx shows clear specificities in the sugar-protein interactions: V-PGal interacts well with PNA and ECA to form aggregates but not with ConA, while V-PGlc interacts with none of the lectins. The results clearly prove that the PV-Gx constructed from the polymers with well-defined sugar units is a new and promising platform for the study of carbohydrate-protein interactions in solution.