Binding and dissociation kinetics using fractals: an analysis of electrostatic effects and randomly coupled and oriented coupled receptors on biosensor surfaces.
A fractal analysis is used to analyze the influence of: (a) electrostatic interactions on binding and dissociation rate coefficients for antibodies HH8, HH10, and HH26 in solution to hen egg-white lysozyme (HEL) immobilized on a sensor chip surface [Biophys. J. 83 (2002) 2946]; and (b) the binding and dissociation of recombinant Fab in solution to random NHS-coupled Cys-HEL and oriented thiol-coupled Cys-HEL immobilized on a sensor chip surface [Methods 20 (2000) 310]. Single- and dual-fractal models were employed to fit the data. Values of the binding and the dissociation rate coefficient(s) and the fractal dimensions were obtained from a regression analysis provided by Corel Quattro Pro 8.0 (Corel Corporation Limited, Ottawa, Canada. 1997). The binding rate coefficients are quite sensitive to the degree of heterogeneity on the sensor chip surface. It is of interest to compare the results obtained by the fractal analysis with that of the original analysis [Biophys. J. 83 (2002) 2946]. For example, as one goes from the binding of 21 nM HH10/HEL to the binding of 640 nM HH10/HEL(K97A), Sinha et al. [Biophys. J. 83 (2002) 29461 indicate that the enhancement of diffusional encounter rates may be due to 'electrostatic steering' (a long-range interaction). Our analysis indicates that there is an increase in the value of the fractal dimension, Df1 by a factor of 1.12 from a value of 2.133-2.385. This increase in the degree of heterogeneity on the surface leads to an increase in the binding rate coefficient, k1 by a factor of 1.59 from 12.92 to 20.57. The fractal analysis of binding and dissociation of recombinant Fab in solution to random NHS-coupled Cys-HEL and oriented thiol-coupled Cys-HEL immobilized on a sensor chip [Methods 20 (2000) 310] surface are consistent with the degree of heterogeneity present on the sensor chip surface for the random and the oriented case. As expected, the random case will exhibit a higher degree of heterogeneity than the oriented case, leading to subsequently a higher binding rate coefficient.
Butala
Harshala D
HD
Chemical Engineering Department, University of Mississippi, Post Office Box 1848, University, MS 38677-1848, USA.
Sadana
Ajit
A
D000906:Antibodies / Q000737:chemistry; D000936:Antigen-Antibody Complex / Q000737:chemistry*; D015374:Biosensing Techniques / Q000295:instrumentation / Q000379:methods*; D003198:Computer Simulation; D004563:Electrochemistry / Q000379:methods*; D019544:Equipment Failure Analysis / Q000379:methods; D017709:Fractals; D007140:Immunoglobulin Fab Fragments / Q000737:chemistry; D007700:Kinetics; D008956:Models, Chemical; D015233:Models, Statistical; D009113:Muramidase / Q000737:chemistry; D011485:Protein Binding; D011956:Receptors, Cell Surface / Q000737:chemistry
D000906:Antibodies; D000936:Antigen-Antibody Complex; D007140:Immunoglobulin Fab Fragments; D011956:Receptors, Cell Surface; C421864:hen egg lysozyme; D009113:Muramidase