| Autor: |
Winder CI; Department of Chemistry, University of Sheffield, Dainton Building, 13 Brook Hill, Sheffield S3 7HF, United Kingdom., Blackburn C; Department of Chemistry, University of Sheffield, Dainton Building, 13 Brook Hill, Sheffield S3 7HF, United Kingdom., Hutchinson CL; Department of Chemistry, University of Sheffield, Dainton Building, 13 Brook Hill, Sheffield S3 7HF, United Kingdom., Shen AQ; Micro/Bio/Nanofluidics Unit, Okinawa Institute of Science and Technology Graduate University, 1919-1 Tancha, Onna-son, Okinawa 904-0495, Japan., Turner NW; Department of Chemistry, University of Sheffield, Dainton Building, 13 Brook Hill, Sheffield S3 7HF, United Kingdom., Sullivan MV; Micro/Bio/Nanofluidics Unit, Okinawa Institute of Science and Technology Graduate University, 1919-1 Tancha, Onna-son, Okinawa 904-0495, Japan. |
| Abstrakt: |
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. |
