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BSA‐imprinted synthetic receptor for reversible template recognition
Author(s) -
Wang Huafang,
He Yunhua,
He Xiwen,
Li Wenyou,
Chen Langxing,
Zhang Yukui
Publication year - 2009
Publication title -
journal of separation science
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.72
H-Index - 102
eISSN - 1615-9314
pISSN - 1615-9306
DOI - 10.1002/jssc.200800562
Subject(s) - molecularly imprinted polymer , chemistry , adsorption , chromatography , monomer , high performance liquid chromatography , substrate (aquarium) , molecular recognition , affinity chromatography , polymer , competitive binding , combinatorial chemistry , molecular imprinting , receptor , molecule , biochemistry , selectivity , organic chemistry , enzyme , catalysis , oceanography , geology
A novel approach to the manufacturing of protein‐responsive imprints on a home‐made chitosan substrate was established together with m ‐aminophenylboronic acid (APBA) as a functional monomer. The produced polymers were characterized using both (1) equilibrium adsorption assays and (2) high performance liquid chromatography analysis. Results confirmed that the synthesized BSA‐MIP (molecularly imprinted polymer) has a high affinity towards its template compared to the determined control proteins. The produced BSA‐MIP featured largely in its good adsorption reversibility, especially in competitive binding assays, which is of great biological significance in separations. Non‐specific binding was reduced to almost zero in a BSA/BHb competitive binding event. An excellent HPLC profile of template recognition was found for BSA‐MIP, even under harsh mobile phase conditions. In the present work, the adopted trapped‐template‐release method permits recovery of bound BSA [1]. The strategy of making an artificial protein‐receptor with high adsorption affinity and reversibility is promising in on‐line isolation of target protein from complicated biological environments.