Determination of protein binding affinities within hydrogel-based molecularly imprinted polymers (HydroMIPs)

EL-Sharif, Hazim F.; Hawkins, Daniel M.; Stevenson, D.; Reddy, Subrayal M.

doi:10.1039/c4cp01798f

Cited by 56 publications

(36 citation statements)

References 23 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…The resultant population of imprinted sites would therefore contain some cavities that are associated with protein clusters. This phenomenon is supported by our previous work[34,35], where force spectroscopy analysis of MIPs suggested that the cavities accommodated an agglomeration of template protein molecules rather than just a single molecule. It is therefore possible that the solution phase represents a more dispersed protein population compared with the original imprinted template population for rebinding protein at low concentrations.…”

supporting

confidence: 78%

MIP-based electrochemical protein profiling

Bueno

EL-Sharif

Salles

et al. 2014

Sensors and Actuators B: Chemical

Self Cite

View full text Add to dashboard Cite

We present the development of an electrochemical biosensor based on modified glassy carbon (GC) electrodes using hydrogel-based molecularly imprinted polymers (MIPs) has been fabricated for protein detection. The coupling of pattern recognition techniques via principal component analysis (PCA) has resulted in unique protein fingerprints for corresponding protein templates, allowing for MIP-based protein profiling. Polyacrylamide MIPs for memory imprinting of bovine haemoglobin (BHb), equine myoglobin (EMb), cytochrome C (Cyt C), and bovine serum albumin (BSA), alongside a non-imprinted polymer (NIP) control, were spectrophotometrically, and electrochemically characterised using modified GC electrodes. Rebinding capacities (Q) were revealed to be higher for larger proteins (BHb and BSA, Q ≈ 4.5) while (EMb and Cyt C, Q ≈ 2.5). Electrochemical results show that due to the selective nature of MIPs, protein arrival at the electrode via diffusion is delayed, in comparison to a NIP, by attractive selective interactions with exposed MIP cavities. However, at lower concentrations such discriminations are difficult due to low levels of MIP rebinding. PCA loading plots revealed 5 variables responsible for the separation of the proteins; E, I, E, I, ΔI . Statistical symmetric measures of agreement using Cohen's kappa coefficient (κ) were revealed to be 63% for bare GC, 96% for NIP and 100% for MIP. Therefore, our results show that with the use of PCA such discriminations are achievable, also with the advantage of faster detection rates. The possibilities for this MIP technology once fully developed are vast, including uses in bio-sample clean-up or selective extraction, replacement of biological antibodies in immunoassays, as well as biosensors for medicine, food and the environment. © 2014 Elsevier B.V

show abstract

supporting

confidence: 78%

MIP-based electrochemical protein profiling

Bueno

EL-Sharif

Salles

et al. 2014

Sensors and Actuators B: Chemical

Self Cite

View full text Add to dashboard Cite

show abstract

“…Along with water solubility, low cost, easy production and engineering are some of polyacrylamide gels’ attractive properties concerning molecular imprinting [46]. Studies on polyacrylamide hydrogel-based MIPs have demonstrated sensitivity and selectivity towards several proteins with different biological roles, sizes and electrochemical activities, namely haemoglobin, myoglobin, cytochrome c, bovine serum albumin (BSA) and catalase [47,48,49]. Further improvements in terms of MIP selectivity have been attempted by including a metal chelating complex comprising bifunctional vinyl groups with the ability to co-polymerize within the polyacrylamide matrix [50].…”

Section: Polymeric Materialsmentioning

confidence: 99%

Imprinting Technology in Electrochemical Biomimetic Sensors

Frasco

Truta

Sales

et al. 2017

Sensors

View full text Add to dashboard Cite

Biosensors are a promising tool offering the possibility of low cost and fast analytical screening in point-of-care diagnostics and for on-site detection in the field. Most biosensors in routine use ensure their selectivity/specificity by including natural receptors as biorecognition element. These materials are however too expensive and hard to obtain for every biochemical molecule of interest in environmental and clinical practice. Molecularly imprinted polymers have emerged through time as an alternative to natural antibodies in biosensors. In theory, these materials are stable and robust, presenting much higher capacity to resist to harsher conditions of pH, temperature, pressure or organic solvents. In addition, these synthetic materials are much cheaper than their natural counterparts while offering equivalent affinity and sensitivity in the molecular recognition of the target analyte. Imprinting technology and biosensors have met quite recently, relying mostly on electrochemical detection and enabling a direct reading of different analytes, while promoting significant advances in various fields of use. Thus, this review encompasses such developments and describes a general overview for building promising biomimetic materials as biorecognition elements in electrochemical sensors. It includes different molecular imprinting strategies such as the choice of polymer material, imprinting methodology and assembly on the transduction platform. Their interface with the most recent nanostructured supports acting as standard conductive materials within electrochemical biomimetic sensors is pointed out.

show abstract

“…In this sense, measurement methods where one of the molecules is immobilized, such as SPR and QCM, may best emulate the release conditions if the method of attachment is the same (30). Other methods include indirect measurement of binding constants by fitting experimental data to adsorption or diffusion models for molecules within the gel (31). For example, the binding constant for a protein immobilized to a gel was measured by observing the diffusion of its binding partner after wetstamping it on specific sites on the gel surface (32).…”

Section: Characterizing Binding Partners For Affinity-controlled Releasementioning

confidence: 98%

Designer protein delivery: From natural to engineered affinity-controlled release systems

Pakulska

Miersch

Shoichet

2016

Science

146

120

View full text Add to dashboard Cite

Exploiting binding affinities between molecules is an established practice in many fields, including biochemical separations, diagnostics, and drug development; however, using these affinities to control biomolecule release is a more recent strategy. Affinity-controlled release takes advantage of the reversible nature of noncovalent interactions between a therapeutic protein and a binding partner to slow the diffusive release of the protein from a vehicle. This process, in contrast to degradation-controlled sustained-release formulations such as poly(lactic-co-glycolic acid) microspheres, is controlled through the strength of the binding interaction, the binding kinetics, and the concentration of binding partners. In the context of affinity-controlled release--and specifically the discovery or design of binding partners--we review advances in in vitro selection and directed evolution of proteins, peptides, and oligonucleotides (aptamers), aided by computational design.

show abstract

Determination of protein binding affinities within hydrogel-based molecularly imprinted polymers (HydroMIPs)

Cited by 56 publications

References 23 publications

MIP-based electrochemical protein profiling

MIP-based electrochemical protein profiling

Imprinting Technology in Electrochemical Biomimetic Sensors

Designer protein delivery: From natural to engineered affinity-controlled release systems

Contact Info

Product

Resources

About