A simple method of controlling the efficiency of surface ligand-cell receptor interaction has been developed in the course of modeling the specific adhesion of cells on a support with their subsequent proliferation and bone tissue formation, using affinity chromatography on macroporous monolithic sorbents. The biospecific peptide GRGDSP played the role of an active ligand on the support, whereas cells were simulated by polymeric (polystyrene) microparticles with the peptide EDYPVDIYYLMDLSYSMKDD immobilized on their surface. The latter peptide is part of the active site of the integrin molecule responsible for binding the RGD sequence. Thus, the monolithic ultrashort column (CIM® disk) represented a simplified model of the support (structural scaffold) possessing biospecific properties. The parameters of the interaction of affinity partners were quantitatively estimated by frontal analysis involving the construction of adsorption isotherms, followed by their linearization and mathematical processing. The data obtained indicate a high specificity of biological pairing, which is supported by the results of cell culture experiments.
| Original language | English |
|---|---|
| Pages (from-to) | 270-276 |
| Number of pages | 7 |
| Journal | Russian Journal of Bioorganic Chemistry |
| Volume | 37 |
| Issue number | 3 |
| DOIs | |
| State | Published - 1 May 2011 |
ID: 35888765