[Macromolecules] From Polymer Sequence Control to Protein Recognition: Synthesis, Self-Assembly and Lectin Binding
writer：Jiawei Lu, Changkui Fu, Shiqi Wang, Lei Tao,* Litang Yan,* David M. Haddleton, Gaojian Chen,* Yen Wei
keywords：http://pubs.acs.org/doi/abs/10.1021/ma500664u
source：期刊
specific source：Macromolecules, Article ASAP DOI: 10.1021/ma500664u
Issue time：2014年
A novel, highly efficient methodology to synthesize gradient
glycopolymers has been successfully developed involving concurrent
enzymatic monomer transformation and reversible addition–fragmentation
chain transfer (RAFT) polymerization. By synchronizing enzymatic monomer
transformation with polymerization, a continuous supply of the second
monomer (glycomonomer) is achieved during the polymerization, resulting
in a gradient sugar distribution in the final polymer. Detailed studies
of the process using GPC and NMR indicate that the gradient
glycopolymers synthesized by RAFT were well controlled. Subsequently,
1,2:3,4-di-O-isopropylidene-6-O-methacryloyl-α-d-galactopyranose
(DIMAG) moieties were deprotected to regenerate the sugar and achieve
amphiphilic bioactive glycopolymers. We demonstrate the synthesis of a
set of glycopolymers with different sequential structures, such as
statistical, gradient and block glycopolymers. The glycopolymers with
block structure show higher affinities toward the RCA120 lectin receptor compared with other structural counterparts.
Furthermore, simulation of the self-assembly of three types of
copolymers and their binding to lectins provides fundamental insight
into this result, revealing the mechanisms underlying the dependence of
self-assembling structures and protein adsorption kinetics on the
molecular architectures of copolymers.