The interaction and kinetic analysis of interleukin-1α and soluble interleukin-1 receptor I

An affinity biosensor based on the resonant mirror was employed to monitor the interaction and kinetic analysis of Interleukin-1 alpha (IL-1 alpha) and type I soluble Interleukin-1 receptor ( sIL-1R I), and the association data between IL-1 alpha and sIL-1R I was fitted by FASTfit software. sIL-1R I was coupled to carboxymethyl dextran (CMD) cuvette surface by the covalent effect of amine to set up the experimental model, with a density of 2. 13 ng/mm(2), which was used to bind to IL-1 alpha in solution. For 2400 nmol/L IL-1 alpha, the response was about 122.66 arc seconds. For the different concentrations of IL-1 alpha, the responses were linear to the concentrations and the linear correlation coefficient was 0. 9972. The binding curve was fitted by FASTfit analysis, which fitted the monophasic association quite well, and the error did not exceed 0.5 arc seconds. For the interaction, K-A was 2.41 x 10(5) (mol/L)(-1), and K-D was 4.15 x 10(-6) mol/L. The experiment verifies the feasibility of using an affinity biosensor to real time monitor the interaction and kinetic analysis of IL-1 alpha and sIL-1R I. All these not only can help to clarify the biological function of IL-1 alpha and sIL-1R I, but also can provide principle and experiment data for the identification and filtration of their effective antagonists.