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Biotechnology and Applied Biochemistry (1999) 29, (45–57) (Printed in Great Britain)

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Analysis of analyte–receptor binding kinetics for biosensor applications: an overview of the influence of the fractal dimension on the surface on the binding rate coefficient

Anand Ramakrishnan and Ajit Sadana¹

Chemical Engineering Department, University of Mississippi, University, MS 38677-9740, U.S.A.

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Abbreviations used: CMD, carboxymethyldextran; GroEL and GroES, two proteins (chaperones) which facilitate protein folding in the cell in an ATP-dependent manner; HSA, human serum albumin; MBP, maltose-binding protein; NTA, nitriloacetic acid; TNF, tumour necrosis factor.

¹ To whom correspondence should be addressed.

An overview of fractal analysis is presented for analyte–receptor binding kinetics for different types of biosensor application. Data taken from the literature can be modelled by using (1) a single-fractal analysis, (2) a single- and a dual-fractal analysis, and (3) a dual-fractal analysis. Cases (2) and (3) represent a change in the binding mechanism as the reaction progresses on the surface. Predictive relationships developed for the binding rate coefficient as a function of the analyte concentration are of particular value because they provide a means by which the binding rate coefficients can be manipulated. Relationships are presented for the binding rate coefficients as a function of the fractal dimension, D_f, or the degree of heterogeneity that exists on the surface. The binding rate coefficient is rather sensitive to the degree of heterogeneity, D_f, that exists on the biosensor surface. For the examples analysed, the order of dependence of the binding rate coefficient on D_f ranges from 1.4770 (k₁), for the binding of intercalators and metabolites in solution to DNA immobilized at a positively charged surface, to 4.9434 for the binding of 5 nM nucleotide+GroEL in solution to GroES immobilized on a Ni²⁺-nitriloacetic acid sensor chip [Nieba, Nieba-Axmann, Persson, Hamalainen, Edebratt, Hansson, Lidholm, Magnusson, Karlsson and Pluckhun (1997) Anal. Biochem. 252, 217–228]. GroEl and GroES are two proteins (chaperones) which facilitate protein folding in the cell in an ATP-dependent manner [Hemmingson, Woolford, van der Vies, Tilly, Dennis, Georgopoulos, Henfrix and Ellis (1988) Nature (London) 333, 330–334]. The overview provides an overall analysis of the reaction parameters of importance observed and how they are influenced in antigen–antibody-binding kinetics for different biosensor applications. The predictive relationships presented provide further physical insights into the binding reactions on the surface, and should assist in enhancing biosensor performance. In general, the technique and the overview presented are applicable for the most part to other reactions occurring on different types of surface, for example cell-surface reactions.

Received 22 May 1998/24 August 1998; accepted 11 September 1998

Portland Press Ltd © 1999