Abstract
Due to recent public concern and interest in the authenticity and origin of meat, for example, the 2013 “horsemeat scandal” in the human food chain, novel sensor strategies for the discrimination between protein species are highly sought after. In this work, molecularly imprinted polymers (MIPs) are utilised for protein discrimination using electrochemical sensor and spectrophotometric techniques. MIP selectivity between two proteins of similar molecular weight (haemoglobin and serum albumin) were compared across three different species, namely pork, beef and human. Bulk MIPs resulted in Kd and Bmax values of 184±23μM, and 582μmolg−1 for BHb, 246.3±26μM, and 673μmolg−1 for HHb; 276±31μM, and 467μmolg−1 for PHb. With the aid of chemometrics, i.e. multivariate analysis and pattern recognition, distinctive protein profiles have been achieved for species discrimination in both spectrophotometric and electrochemical analysis experiments. MIP suitability and selectivity within complex matrices was also assessed using urine, human plasma and human serum. Pattern recognition MIP-based protein profiling demonstrated positive outputs yielding either a ‘bovine’ or ‘not-bovine’ outcome (p=0.0005) for biological samples spiked with/without bovine using respective bovine haemoglobin MIPs.
Highlights
Proteins are essential parts of organisms and participate in virtually every process within cells 1
The molecular imprinting effect or imprinting efficiency is characterised by the rebinding capacity (Q) of template to the polymer gel exhibited by the template-specific molecularly imprinted polymers (MIPs)
This is calculated using equation 1, where Ci and Cf are the initial template and the recovered template concentrations respectively, V is the volume of the initial solution, and g is the mass of the gel polymers (g)
Summary
Proteins are essential parts of organisms and participate in virtually every process within cells 1. A large number of proteins are vital markers of disease. The development of biosensor strategies for the detection of proteins is imperative for applications in proteomics, medical diagnostics, and pathogen detection 3. Molecularly imprinted polymers (MIPs) have been developed for the imprinting of proteins, and are rapidly becoming viable alternatives to natural antibodies for sensor technology 2, 4-7. The imprinting of large biomacromolecules, such as proteins, presents a variety of challenges. Due to the large size of proteins (~6000 Da to several million Da) it is essential to control the size and number of pores that are generated (in the bulk and on the surface) during MIP synthesis, together with the density of MIP network 12
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