Mlcrofluidic tools for studying the specific binding, adsorption, and displacement of proteins at interfaces

Matthew A. Holden, Paul S. Cremer

Research output: Contribution to journalArticle

20 Scopus citations

Abstract

A combination of temperature and concentration gradient microfluidic devices were employed to study the mechanistic details of biomacromolecule interactions at oxide interfaces. These lab-on-a-chip techniques allowed high-throughput, multiplexed data collection using only nanoliters of analyte. The three examples presented demonstrate rapid data acquisition relative to standard methods. First, we show ligand-receptor binding data for multivalent binding between membrane-bound ligands and incoming aqueous proteins with several binding pockets. A model is described for obtaining both the first and second dissociation constant for the reaction. The second example employs temperature gradient microfluidics to study the thermoresponsive properties of polymers and proteins. Both the folding mechanism and subsequent formation of an aqueous two-phase system were followed. Finally, these microfluidic techniques were combined with fluorescence microscopy and nonlinear optical spectroscopy to elucidate the mechanism of fibrinogen displacement from silica surfaces. This combination of methods enabled both direct and indirect observation of protein conformational changes.

Original languageEnglish (US)
Pages (from-to)369-387
Number of pages19
JournalAnnual Review of Physical Chemistry
Volume56
DOIs
StatePublished - Aug 26 2005

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All Science Journal Classification (ASJC) codes

  • Physical and Theoretical Chemistry

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