Share Email Print
cover

Proceedings Paper

Fractal binding and dissociation kinetics of lecithin cholesterol acyl transferase (LCAT), a heart-related compound, on biosensor surfaces
Author(s): Atul M. Doke; Ajit Sadana
Format Member Price Non-Member Price
PDF $14.40 $18.00
cover GOOD NEWS! Your organization subscribes to the SPIE Digital Library. You may be able to download this paper for free. Check Access

Paper 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.

Paper Details

Date Published: 19 May 2006
PDF: 14 pages
Proc. SPIE 6218, Chemical and Biological Sensing VII, 621815 (19 May 2006); doi: 10.1117/12.664724
Show Author Affiliations
Atul M. Doke, Univ. of Mississippi (United States)
Ajit Sadana, Univ. of Mississippi (United States)


Published in SPIE Proceedings Vol. 6218:
Chemical and Biological Sensing VII
Patrick J. Gardner; Augustus W. Fountain, Editor(s)

© SPIE. Terms of Use
Back to Top