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Charged groups synergically enhance protein imprinting in amphoteric polyacrylamide cryogels
Author(s) -
Yang Chun,
Zhou XingLu,
Liu YaRu,
Wang Jian,
Tian LiLi,
Zhang Yan,
Hu XiaYa
Publication year - 2016
Publication title -
journal of applied polymer science
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.575
H-Index - 166
eISSN - 1097-4628
pISSN - 0021-8995
DOI - 10.1002/app.43851
Subject(s) - acrylic acid , acrylamide , monomer , polyacrylamide , polymer , bovine serum albumin , polymer chemistry , polyelectrolyte , molecular imprinting , chemical engineering , imprinting (psychology) , molecularly imprinted polymer , chemistry , materials science , selectivity , chromatography , organic chemistry , biochemistry , engineering , catalysis , gene
Proteins are amphoteric biopolymers with unevenly charged exterior surfaces. Taking this point fully into account could accomplish ingenious recognition systems for the biological macromolecues. Molecularly imprinted polymers (MIPs) are good tools to study the interactions between polymeric matrices and template molecules. Here different protein imprinted cryogels were prepared. Imprinting factors (IFs) were determined with bovine serum albumin (BSA) as the template. The IF of the polymeric cryogel made from only acrylamide (AM) and N,N′‐methylenebisacrylamide (BisAM) is about 1.38. The introduction of charged monomers, either acrylic acid or diallylamine, would increase IFs obviously. One of the basic cryogels gave the maximum IF (about 2.0) of that type. As both acrylic acid and diallylamine were involved, IFs were further increased. An amphoteric cryogel with a suitable acid‐base ratio gave a high IF of about 3.7. Whatever used alone or both, too many added acidic or basic monomers resulted in IF reduction. Taking full advantage of charged groups in MIPs could be a good way to manipulate protein–polymer interactions. © 2016 Wiley Periodicals, Inc. J. Appl. Polym. Sci. 2016 , 133 , 43851.