Droplet microfluidic systems provide a controlled environment in which to perform rapid mixing, isolation of picoliter size fluid volumes and rapid variation of reaction conditions. Indeed, the ability to controllably form droplets with variable reagent composition at high speed lies at the heart of performance improvements when compared to conventional microfluidic devices operating under laminar flow conditions. Furthermore, it is important to realize that segmented-flow systems can generate droplets at rates in excess of 1 kHz. In theory, this means that millions of individual reactions or assays can be processed in very short times. In addition, since mixing is rapid and reagent transport occurs with no dispersion, microdroplet reactors are superior environments in which to study biological reactions, especially rapid kinetic reactions, when compared to diffusion-limited continuous-flow formats. Accordingly, droplet microfluidics is a promising technology to perform reactions and assays in a high-throughput manner, in which a hugely productive and efficient system for screening a desired component from thousands of samples is necessary.
This is a preview of subscription content, log in to check access.
Springer Nature is developing a new tool to find and evaluate Protocols. Learn more
M. Srisa-Art would like to thank Prof Andrew J. deMello and Dr Joshua B. Edel for their supervision, advice, and encouragement and also acknowledge the Royal Thai Government for provision of a research scholarship. This work was supported by the EPSRC and the RCUK Basic Technology Programme.
Griffiths AD, Tawfik DS (2006) Miniaturising the laboratory in emulsion droplets. Trends Biotechnol 24:395–402CrossRefGoogle Scholar
Kelly BT et al (2007) Miniaturizing chemistry and biology in microdroplets. Chem Commun:1773–1788Google Scholar
Taly V, Kelly BT, Griffiths AD (2007) Droplets as microreactors for high-throughput biology. Chembiochem 8:263–272CrossRefGoogle Scholar
Piran U, Riordan WJ (1990) Dissociation rate-constant of the biotin-streptavidin complex. J Immunol Methods 133:141–143CrossRefGoogle Scholar
Bayer EA, Wilchek M (1990) Biotin-binding proteins—overview and prospects. Methods Enzymol 184:49–51CrossRefGoogle Scholar
Chilkoti A, Stayton PS (1995) Molecular-origins of the slow streptavidin-biotin dissociation kinetics. J Am Chem Soc 117:10622–10628CrossRefGoogle Scholar
Livnah O et al (1993) 3-Dimensional structures of avidin and the avidin-biotin complex. Proc Natl Acad Sci U S A 90:5076–5080CrossRefGoogle Scholar
Goodrich JA, Kugel JF (2007) Binding and kinetics for molecular biologists. Cold Spring Harbor, New YorkGoogle Scholar
Oshannessy DJ et al (1993) Determination of rate and equilibrium binding constants for macromolecular interactions using surface-plasmon resonance—use of nonlinear least-squares analysis-methods. Anal Biochem 212:457–468CrossRefGoogle Scholar
Edwards PR, Leatherbarrow RJ (1997) Determination of association rate constants by an optical biosensor using initial rate analysis. Anal Biochem 246:1–6CrossRefGoogle Scholar
Edwards PR et al (1995) Kinetics of protein-protein interactions at the surface of an optical biosensor. Anal Biochem 231:210–217CrossRefGoogle Scholar
Gonzalez M et al (1997) Interaction of biotin with streptavidin—thermostability and conformational changes upon binding. J Biol Chem 272:11288–11294CrossRefGoogle Scholar
Buranda T et al (1999) Ligand receptor dynamics at streptavidin-coated particle surfaces: a flow cytometric and spectrofluorimetric study. J Phys Chem B 103:3399–3410CrossRefGoogle Scholar