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

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.

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Publication Details

Journal
Biomacromolecules
Published
2024-10-31
DOI
https://doi.org/10.1021/acs.biomac.4c01097
Citations
1
Primary Topic
Analytical chemistry methods development
Type
article
Field-Weighted Citation Impact
0.24

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article

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

Chester Blackburn, Nicholas W. Turner, Amy Q. Shen, Mark V. Sullivan et al.
1 citations
Biomacromolecules
Analytical chemistry methods development
0.24
article

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

Chester Blackburn, Nicholas W. Turner, Amy Q. Shen, Mark V. Sullivan, Christopher Hutchinson, Christoph Winder
article en
1 citations

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.

BiomacromoleculesVol. 25(11)
Okinawa Institute of Science and Technology Graduate University (JP), University of Sheffield (GB)
University of Sheffield, Okinawa Institute of Science and Technology Graduate University, Engineering and Physical Sciences Research Council
Openalex Percentile: Top 50%
Analytical chemistry methods development
0.24
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Enzyme Activity Inhibition of α-Amylase Using Molecularly Imprinted Polymer (MIP) Hydrogel Microparticles — Chester Blackburn, Nicholas W. Turner, et al. · Biomacromolecules (2024) | TGRS Research Map | TGRS