Study of the interactions between protein-imprinted hydrogels and their templates.
The interactions between lysozyme-imprinted hydrogel and their template protein were studied using adsorption measurements, competitive adsorption experiments, and isothermal titration calorimetry (ITC). The results were compared to the interactions between the imprinted polymer and a reference protein, cytochrome c. Experimental adsorption isotherms and competitive adsorption studies detected better affinity and higher capacity of the imprinted polymer toward the template protein. Moreover, analysis of ITC data identified major differences in the binding enthalpy of lysozyme when the imprinted and the non-imprinted polymers were compared. On the other hand, cytochrome C did not exhibit any major changes in the adsorption enthalpy when comparing the imprinted and the non-imprinted polymers. This is the first thermodynamic evidence for the creation of new binding sites in the process of protein imprinting.
Kimhi
Ohad
O
The Inter-Departmental Program for Biotechnology, The Russell Berrie Nanotechnology Institute, and Department of Chemical Engineering, Technion-Israel Institute of Technology, Haifa 32000, Israel.
Bianco-Peled
Havazelet
H
D000327:Adsorption; D000818:Animals; D001665:Binding Sites; D002151:Calorimetry; D045304:Cytochromes c / Q000737:chemistry; D020100:Hydrogels / Q000737:chemistry; D066298:In Vitro Techniques; D008855:Microscopy, Electron, Scanning; D008958:Models, Molecular; D018716:Molecular Mimicry; D046912:Multiprotein Complexes / Q000737:chemistry; D009113:Muramidase / Q000737:chemistry; D011485:Protein Binding; D011487:Protein Conformation; D011506:Proteins / Q000737:chemistry*; D055672:Static Electricity
D020100:Hydrogels; D046912:Multiprotein Complexes; D011506:Proteins; D045304:Cytochromes c; D009113:Muramidase