Proteins are increasingly being used in numerous technological applications such as biosensors, biofuel cells and biocatalysts. Often the immobilization of a protein in a synthetic matrix is essential.1,2 Porous matrices have warranted much attention due numerous factors, such as their high surface areas, meaning improved protein loading and high number of active sites; the protection of the protein in the pores from possible bacterial degradation; and/or for the controlled release of the proteins.
Nevertheless, the incorporation of a protein in a porous material is nontrivial. In fact, the preparation of such protein loaded materials is often limited by the size compatibility between the pore and the protein, the surface properties (charge and hydrophobicity) and experimental parameters such as pH and ionic strength.3,4 Moreover, the quest for a suitable protein-porous matrix combination not only require the synthesis of matrices with tailored textural properties, but also the development of appropriate methodologies that can be used to determine the effect of the synthetic matrix on the structure and stability of the protein.
Recently, we have been interested in the incorporation of human neuroglobin (NGB) into mesoporous silica (SBA-15) and titania with potential application in biosensing. Using EPR, we have monitored conformational changes to the NGB heme-pocket upon incorporation and subsequent manipulations. We have also performed site-directed mutagenesis and spin labeling, and have compared the mobility and structure of free and immobilized NGB using EPR. These results will be presented.
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- S. Loreto, et al., PCCP, 2017, 19, 13503
- S. Loreto, et al., J. Phys. Chem. C, 2018, 122, 41