Abstract
Proteins play a major role in biosensors in which they provide catalytic activity and specificity in molecular recognition. However, the immobilization process is far from straightforward as it often affects the protein functionality. Extensive interaction of the protein with the surface or significant surface crowding can lead to changes in the mobility and conformation of the protein structure. This review will provide insights as to how an analysis of the physico-chemical features of the protein surface before the immobilization process can help to identify the optimal immobilization approach. Such an analysis can help to preserve the functionality of the protein when on a biosensor surface.
Highlights
Proteins provide specific recognition for the analyte in biosensors and their immobilization is a crucial component: it can highly affect the performance of the device if electron transfer is not guaranteed or if the protein undergoes major conformational changes that alter its functionality
As compared to small molecules that offer few chemical groups of clear position and solvent accessibility, protein sizes can reach the tens of nanometers and achieve complex three-dimensional structures that dynamically move during bioactivity, with environmental conditions, and especially after coming into contact with material surfaces
To achieve optimal immobilization in a biosensor can be a complex task, one which often proceeds through trial and error to retain most of the affinity for either the analyte or, in the case of enzymes, enzymatic activity
Summary
Proteins provide specific recognition for the analyte in biosensors and their immobilization is a crucial component: it can highly affect the performance of the device if electron transfer is not guaranteed or if the protein undergoes major conformational changes that alter its functionality. Immobilization in a preferred orientation can guarantee the maximal exposure of biorecognition moieties, e.g., catalytic sites of enzymes and antigen-binding sites of antibodies [5], while the protein region interacting with the surface is minimized and limited to regions of the molecule that do not undergo conformational changes during biorecognition. Oriented immobilization of enzymes has been proven to lead to a higher catalytic activity on the surface as compared to random immobilization [6]. An overview of the developed strategies of proteins immobilized and their outcome are discussed
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