NDLI: Affinity-tunable specific recognition of glycoproteins <i>via</i> boronate affinity-based controllable oriented surface imprinting

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Chemical Science Vol - 5 Issue - 2

Chemical Science Vol -4

Chemical Science Vol -3

Chemical Science Vol -2

Chemical Science Vol -1

Affinity-tunable specific recognition of glycoproteins via boronate affinity-based controllable oriented surface imprinting

Content Provider	Royal Society of Chemistry (RSC)
Author	Ye, Jin Bie, Zijun Liu, Zhen Wang, Shuangshou
Copyright Year	2014
Abstract	The molecular imprinting of proteins is of great importance but remains a challenge. Particularly, efficient, universal and facile approaches for protein imprinting are limited. Here we report a new general approach, boronate affinity-based controllable oriented surface imprinting, for the efficient and facile imprinting of glycoproteins. A glycoprotein template was first covalently anchored onto the surface of a boronic acid-functionalized substrate by boronate affinity binding. The substrate surface was then deposited with a thickness-controllable imprinting coating generated by in-water self-copolymerization of dopamine and m-aminophenylboronic acid (APBA). After removal of the template with an acidic solution, 3D cavities complementary to the molecular shape of the template were formed in the imprinting layer. The imprinting layer was hydrophilic and showed limited residual boronic acid, thus non-specific binding was avoided. The approach has significant advantages, including high specificity, high imprinting efficiency, and widely applicable substrates (from 2D to 3D, from regular size to nanoscale). Uniquely, the prepared molecularly imprinted polymers can rebind the templates in dual modes: a high affinity mode (boronate affinity interaction is on) and a low affinity mode (boronate affinity interaction is off), and the overall binding strength can be tuned by adjusting the surrounding pH. Such an affinity-tunable dual-mode binding mechanism enables the binding strength to be adjusted while keeping the specificity, which allows for wider applications, and also sheds new light on the role of affinity-determining factors in molecular imprinting.
Starting Page	1135
Ending Page	1140
Page Count	6
File Format	HTM / HTML PDF
ISSN	20416520
Volume Number	5
Issue Number	3
Journal	Chemical Science
DOI	10.1039/c3sc52986j
Language	English
Publisher	Royal Society of Chemistry
Access Restriction	Open
Subject Keyword	APBA Acid Dopamine Glycoprotein PH Hydrophile Molecular imprinting American Power Boat Association Protein Three-dimensional space
Content Type	Text
Resource Type	Article
Subject	Chemistry

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