Fractal binding and dissociation kinetics of lecithin cholesterol acyl transferase (LCAT), a heart-related compound, on biosensor surfaces

Atul M. Doke; Ajit Sadana

doi:10.1117/12.664724

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19 May 2006 Fractal binding and dissociation kinetics of lecithin cholesterol acyl transferase (LCAT), a heart-related compound, on biosensor surfaces

Atul M. Doke, Ajit Sadana

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Proceedings Volume 6218, Chemical and Biological Sensing VII; 621815 (2006) https://doi.org/10.1117/12.664724
Event: Defense and Security Symposium, 2006, Orlando (Kissimmee), Florida, United States

Abstract

A fractal analysis is presented for the binding and dissociation of different heart-related compounds in solution to receptors immobilized on biosensor surfaces. The data analyzed include LCAT (lecithin cholesterol acyl transferase) concentrations in solution to egg-white apoA-I rHDL immobilized on a biosensor chip surface.¹ Single- and dual- fractal models were employed to fit the data. Values of the binding and the dissociation rate coefficient(s), affinity values, and the fractal dimensions were obtained from the regression analysis provided by Corel Quattro Pro 8.0 (Corel Corporation Limited).² The binding rate coefficients are quite sensitive to the degree of heterogeneity on the sensor chip surface. Predictive equations are developed for the binding rate coefficient as a function of the degree of heterogeneity present on the sensor chip surface and on the LCAT concentration in solution, and for the affinity as a function of the ratio of fractal dimensions present in the binding and the dissociation phases. The analysis presented provided physical insights into these analyte-receptor reactions occurring on different biosensor surfaces.

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Atul M. Doke and Ajit Sadana "Fractal binding and dissociation kinetics of lecithin cholesterol acyl transferase (LCAT), a heart-related compound, on biosensor surfaces", Proc. SPIE 6218, Chemical and Biological Sensing VII, 621815 (19 May 2006); https://doi.org/10.1117/12.664724

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