Mary J. Wirth

This is the second in a four-part series of articles exploring topics that will be addressed at the HPLC 2016 conference in San Francisco, USA, from 19–24 June.

Separations of intact proteins play many roles in drug discovery and development. A variety of separation techniques are used, from immunoprecipitation for study of a single protein of interest, through various types of column chromatography for detecting a handful of proteins at once, all the way to proteomics for studying hundreds to thousands of proteins. What all of these techniques and applications have in common is that the power of protein separations is limited by the fact that proteins are large, slowly diffusing, sticky molecules. This article discusses various chromatographic approaches to addressing this challenge. This is the second in a series of articles exploring topics that will be addressed at the HPLC 2016 conference in San Francisco, from June 19 to 24.

Professor Mary Wirth and graduate students Bingchuan Wei and Benjamin Rogers from Purdue University demonstrate a quantum leap in protein column efficiency. Using colloidal silica particles of submicrometer diameters (470 nm), they obtained plate heights that were as much as 15-fold lower than the theoretical limit for Hagen-Poiseuille flow.