Many of the readers of F-Blog may not be familiar with field of proteomics, since we have a tendency to be more chemistry-centric, but it’s a fascinating area and fast moving area of research. Just available online is a short review in Analytical Chemistry from Figeys and co-workers entitled Proteomics: From Technology Development to Biological Applications. This review provides a relatively quick synopsis of the various sub-disciplines within proteomics and the techniques being used today within those sub-disciplines. It covers quantitative proteomics, protein-protein interactions, post-translational modifications (PTMs), and chemical proteomics as the sub-disciplines and then moves to the tools used such as LC/MS, bioinformatics, and database management.
As one reads through the review you realize the importance of sample enrichment and separations in proteomics. That, of course, is where fluorous comes in. The vastness and complexity of the proteome makes enrichment a vital strategy in simplifying a sample for analysis. For example, if you’re looking to study glycosylation as a post-translational modification, you want to be able to examine just those proteins that are glycosylated. So methods which separate the glycosylated proteins from all the non-glycosylated ones are devised. (Later this week, we’ll publish a blog post about just such a strategy.) The most common method for enrichment is to use some sort of affinity chromatography. Biotin, His-tags, IMAC, are all popular methods.
Fluorous has been used also in this regard, although not as extensively as we’d like up to this point, but we think we’re making up ground. There’s a brief nod to fluorous techniques within the review, but I believe the reference is incorrect. (They meant to cite this reference to fluorous enrichment, but cited this one instead.) Fluorous enrichments have the advantage of low non-specific binding, excellent MS characteristics, and complete compatibility with standard protein identification software.