Analyte–receptor binding on surface plasmon resonance biosensors: a fractal analysis of Cre– loxP interactions and the influence of Cl, O, and S on drug–liposome interactions

Abstract

A fractal analysis of the association and dissociation (whereever applicable) of Cre– loxP interactions and drug–liposome interactions on a sensor chip surface is presented. In both of these cases a dual-fractal analysis is required to adequately describe the association kinetics. The dissociation kinetics for Cre– loxP interactions is adequately described by a single-fractal analysis. The dual-fractal analysis used to describe the association kinetics of Cre– loxP interactions is consistent with the original two-step mechanism presented using a surface plasmon resonance biosensor. Our analysis includes both diffusion and surface effects by introducing the fractal dimension which makes quantitative the degree of heterogeneity on the sensor chip surface. Affinities are provided. Only the association kinetics were analysed for drug–liposome interactions since the initial sections of the dissociation curves were too steep to obtain reasonable drug–liposome complex concentration values on the sensor chip with time. Attempts made to relate the association rate coefficients with the molecular weight of the drug were unsuccessful. On using desipramine and imipramine as “arbitrarily selected standards” or “references” (only C, H, and N atoms present), it was noticed from the data analysed that the inclusion of the O and S atoms in the drug leads to a decrease in the association rate coefficients, k a1 (or k 1) and k a2 (or k 2) (compared with the arbitrarily selected standards or references). Similarly, the addition of the Cl atom in the drug leads to an increase in the association rate coefficient (compared with the arbitrarily selected standards or references). More data needs to be analysed to determine whether this is true for other drugs also.