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Enzyme Activity Inhibition of α-Amylase Using Molecularly Imprinted Polymer (MIP) Hydrogel Microparticles.

Authors :
Winder CI
Blackburn C
Hutchinson CL
Shen AQ
Turner NW
Sullivan MV
Source :
Biomacromolecules [Biomacromolecules] 2024 Nov 11; Vol. 25 (11), pp. 7459-7465. Date of Electronic Publication: 2024 Oct 31.
Publication Year :
2024

Abstract

Molecularly imprinted polymers (MIPs) are a class of synthetic recognition materials that offer a cost-effective and robust alternative to antibodies. While MIPs have found predominant use in biosensing and diagnostic applications, their potential for alternative uses, such as enzyme inhibition, remains unexplored. In this work, we synthesized a range of acrylamide-based hydrogel MIP microparticles (35 μm) specific for the recognition of α-amylase. These MIPs also showed good selectivity toward the target protein with over 96% binding of the target protein, compared with the control nonimprinted polymer (NIP) counterparts. Specificity of the MIPs was determined with the binding of nontarget proteins, trypsin, human serum albumin (HSA), and bovine serum albumin (BSA). The MIPs were further evaluated for their ability to inhibit α-amylase enzymatic activity, showing a significant decrease in activity. These findings highlight the potential of MIPs as enzyme inhibitors, suggesting an innovative application beyond their conventional use.

Details

Language :
English
ISSN :
1526-4602
Volume :
25
Issue :
11
Database :
MEDLINE
Journal :
Biomacromolecules
Publication Type :
Academic Journal
Accession number :
39479798
Full Text :
https://doi.org/10.1021/acs.biomac.4c01097