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Physical Methods for Studying Drug-Protein Binding

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Concepts in Biochemical Pharmacology

Abstract

The techniques which are available for studying drug binding to proteins and other macromolecules can be divided into two broad categories (i) nonspectroscopic methods (ii) spectroscopic methods (Table 1). The first group contains many of the classical techniques for studying drug binding, including equilibrium dialysis, ultrafiltration and ultracentrifugation. Since these techniques have been adequately dealt with elsewhere (Rosenburg and Klotz, 1960; Goldstein, 1949) they will not be covered in this chapter except to point out three more recent methods, rapid (or kinetic) dialysis, gel filtration, and microcalorimetry. Instead, emphasis will be placed on spectroscopic techniques since they can measure not only drug binding, but can also probe the interactions of drugs with biological systems at a molecular level (Chignell, 1970 C).

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  1. Colin F. Chignell
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  1. Department of Health, Education and Welfare, National Institutes of Health, 20014, Bethesda, MD, USA

    Bernard B. Brodie  & James R. Gillette  & 

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Chignell, C.F. (1971). Physical Methods for Studying Drug-Protein Binding. In: Brodie, B.B., Gillette, J.R., Ackerman, H.S. (eds) Concepts in Biochemical Pharmacology. Handbuch der experimentellen Pharmakologie/Handbook of Experimental Pharmacology, vol 28 / 1. Springer, Berlin, Heidelberg. https://doi.org/10.1007/978-3-642-65052-9_9

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