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A major factor in the design of highly sensitive ligand-binding assays is the need to accelerate the interaction between analyte and binding partner (or capture reagent). In early immunoassay technologies, overnight incubations with exogenously supplied binding partners at low temperatures (typically 2–8 °C) were common. More recently, however, assay results are frequently required, for both medical and commercial reasons, within a relatively short time (∼1–2 h). The need to accelerate the binding reaction is certainly becoming even more important as high-throughput instruments (where minutes are the more common time frame) become widely utilized. This problem is typically addressed in commercial instruments by adding a large excess of the exogenous binding partner or using less than optimum temperature conditions so as to drive the binding reaction as far as possible in an acceptable assay time.High hydrostatic pressure is a powerful tool for studying the structure and function of proteins (1)(2). Very high pressures cause most proteins to denature because of irreversible changes in the secondary and tertiary structure (3). At less than the denaturation pressure, the tertiary and secondary nature of proteins are reversibly affected by changes in hydrostatic pressure (3). Although some commercial applications of high hydrostatic pressure in the field of biotechnology have been reported or proposed (4)(5), its use to control or modulate biomolecular interactions of commercial interest has received little attention to date. Here, we describe the use of high hydrostatic pressure to considerably accelerate the kinetics of …

Use of High Pressure to Accelerate Antibody:Antigen Binding Kinetics Demonstrated in an HIV-1 p24:Anti-HIV-1 p24 Assay