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Formaldehyde Case Study

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Formaldehyde Case Study
Formaldehyde as a model protein crosslinking reagent.
Understanding protein-protein interactions is becoming a vital study for application in the development of new age pharmaceuticals and utilization in diagnostic models. The overall aim is to gain an insight into the function and role of individual proteins with specific interest on how they react in cells, (Toews et al. 2008). The biopharma industry in Ireland is becoming a booming success for the economy therefore a complete understanding of how proteins interact in vivo is essential to the development of newer and better technologies. Chemical cross-linking of proteins has been a long established technique with the ultimate goal of covalently linking amino acid side chains of a particular protein and inducing an increased stability on the overall structure of the targeted amino acid or protein side chain,(Means & Feeney 1990).
Formaldehyde has been utilized for protein cross-linking for a long time. It is now becoming a novel approach for the studying of protein-protein interactions in living cells, (Toews et al. 2008). Formaldehydes relatively
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In vitro studies have shown that the main cross-link reactions develop on amino and thiol groups of arginine, cysteine, lysine, histidine and tryptophan residues, (Metz 2003; Metz et al. 2006). While in the in vivo studies performed by Toews et al. 2008 show the N-terminus a main target and also agreed with studies done by Metz et al. finding consistent modifications to lysine, and tryptophan with particular emphasis on the amino termini and side chains. Further work by this group in 2010 confirmed these results further and deduced cysteine is a dominant reactive site particularly in conditions similar to intracellular protein reactions, (Toews et al.

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