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Topological Glycopolymers as Agglutinator and Inhibitor: Cyclic versus Linear
Author(s) -
Liu Lei,
Zhou Feng,
Hu Jun,
Cheng Xiaoxiao,
Zhang Wei,
Zhang Zhengbiao,
Chen Gaojian,
Zhou Nianchen,
Zhu Xiulin
Publication year - 2019
Publication title -
macromolecular rapid communications
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.348
H-Index - 154
eISSN - 1521-3927
pISSN - 1022-1336
DOI - 10.1002/marc.201900223
Subject(s) - glycopolymer , chemistry , galactose , topology (electrical circuits) , cyclic peptide , polymerization , amyloid (mycology) , biophysics , combinatorial chemistry , stereochemistry , biochemistry , peptide , polymer , organic chemistry , biology , mathematics , inorganic chemistry , combinatorics
Carbohydrates play an important role in biological processes for their specific interactions with proteins. Cyclic glycopolymers are promising to mimic the topology of natural macrocycle–biomacromolecules due to their unique architecture of lacking chain ends. To systematically study the effect of glycopolymer architecture on the interactions with protein, the cyclic glycopolymers bearing galactose side‐chain (cyclic PMAG n ) with three degrees of polymerization ( n = 14, 24, 47) are prepared for the first time. The cyclic PMAG n exhibits unique properties in agglutinating and inhibiting proteins in subsequent studies by comparison with the linear precursor with the same molecular weights. More impressively, the cyclic PMAG n highlight the improved performance of cyclic architecture. For example, the cyclic PMAG n shows superior inhibition abilities to suppress amyloid formation from amyloid β protein fragment 1‐42 aggregation and block the specific interaction between bacteria and galactose‐modified surface compared to that of respective linear counterpart. This interesting finding suggests that the architecture of cyclic glycopolymers may be capable of optimizing the ability to bind or inhibit proteins in biological processes.