Related Experiment Video
Updated: May 4, 2026

11:31
Preparation of Hydroxy-PAAm Hydrogels for Decoupling the Effects of Mechanotransduction Cues
Published on: August 28, 2014
13.0K
Enhanced selectivity of hydrogel-based molecularly imprinted polymers (HydroMIPs) following buffer conditioning
Hazim F El-Sharif1, Quan T Phan1, Subrayal M Reddy1
1Department of Chemistry, Faculty of Engineering and Physical Sciences, University of Surrey, Guildford, Surrey GU2 7XH, UK.
Analytica Chimica Acta
|January 15, 2014
Summary
Optimizing buffer conditions, particularly using Tris buffer at pH 7.4, significantly enhances molecularly imprinted polymer (MIP) selectivity for protein binding. Proper conditioning prevents negative impacts on imprinting capability, crucial for real-world applications.
Area of Science:
- Polymer Chemistry
- Bioseparation Science
- Analytical Chemistry
Background:
- Molecularly imprinted polymers (MIPs) offer selective recognition of target molecules.
- Optimizing MIP performance requires careful consideration of buffer conditions during synthesis and use.
- Previous studies have not fully elucidated the impact of buffer composition and pH on MIP selectivity for specific protein targets.
Purpose of the Study:
- To investigate the effect of buffer solution composition and pH on the selectivity of acrylamide-based MIPs.
- To determine optimal buffer conditions for the preparation, washing, and re-loading phases of MIPs for protein imprinting.
- To evaluate the impact of buffer conditioning on MIP performance in real biological samples.
Main Methods:
- Synthesized acrylamide-based MIPs for bovine haemoglobin (BHb), equine myoglobin (EMb), and bovine catalyse (BCat).
- Tested various buffer solutions including water, phosphate buffer saline (PBS), Tris buffer, and succinate buffer at different pH levels.
- Assessed MIP selectivity by comparing binding affinities to target proteins versus non-target proteins (NIPs) under varied buffer conditions.
Main Results:
- Acrylamide-based MIPs showed highest selectivity, with Tris buffer at 50 mM and pH 7.4 yielding optimal imprinting conditions.
- MIP selectivity decreased with buffer conditions and pH in the order of Tris > PBS > succinate.
- Re-loading buffer conditions were found to be more critical than preparation conditions for MIP selectivity.
- Protein re-loading in water after conditioning with Tris or PBS (pH 7.4) significantly reduced MIP selectivity.
- Acidifying buffer pH below 5.9 negatively impacted MIP selectivity, especially for proteins with high isoelectric points.
Conclusions:
- Buffer composition and pH play a critical role in determining the selectivity of acrylamide-based MIPs for protein imprinting.
- Tris buffer at pH 7.4 provides optimal conditions for enhancing MIP selectivity.
- Proper buffer conditioning is essential for maintaining MIP imprinting capability, with implications for applications in real biological samples like plasma and serum.

