Journal
BIOMACROMOLECULES
Volume 13, Issue 12, Pages 3959-3965Publisher
AMER CHEMICAL SOC
DOI: 10.1021/bm301189f
Keywords
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Funding
- U.K. Engineering and Physical Sciences Research Council (EPSRC) [EP/G014299/1, EP/G014736/1, EP/G027005]
- EPSRC [EP/G014736/1, EP/G027005/1, EP/G014299/1] Funding Source: UKRI
- Engineering and Physical Sciences Research Council [EP/G027005/1, EP/G014299/1, EP/G014736/1] Funding Source: researchfish
- Natural Environment Research Council [1232404] Funding Source: researchfish
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We have characterized the imprinting capability of a family of acrylamide polymer-based molecularly imprinted polymers (MIPs) for bovine hemoglobin (BHb) and trypsin (Tryp) using spectrophotometric and quartz crystal microbalance (QCM) sensor techniques. Bulk gel characterization on acrylamide (AA), N-hydroxymethylacrylamide (NHMA), and N-isopropylacrylamide (NiPAM) gave varied selectivities when compared with nonimprinted polymers. We have also harnessed the ability of the MIPs to facilitate protein crystallization as a means of evaluating their selectivity for cognate and noncognate proteins. Crystallization trials indicated improved crystal formation in the order NiPAM < AA < NHMA. QCM studies of thin film MIPs confirm this trend with N-hydroxymethyl acrylamide MIPs exhibiting best discrimination between MIP and NIP and also cognate/noncognate protein loading. Equivalent results for acrylamide MIPs suggested that the cavities were equally selective for both proteins, while N-isopropylacrylamide MIPs were not selective for either cognate BHb or noncognate BSA. All BHb MIP-QCM sensors based on AA, NHMA, or NiPAM were essentially nonresponsive to smaller, proteins. Protein crystallization studies validated the hydrophilic efficacy of MIPS indicated in the QCM studies.
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