Limited Proteolysis (LiP)

Unbiased and proteome-wide profiling of protein conformational changes

Limited Proteolysis (LiP) technology enables the unbiased and proteome-wide profiling of protein conformational changes. Protein conformational changes can result from a variety of stimuli such as heat shock, protein-protein interactions, compound binding, posttranslational modifications, etc. These conformational changes can be probed using limited proteolysis (LiP) since protein conformational changes will affect the kinetics of the proteolytic cleavage during the LiP reaction.

LiP reactions are carried out on native proteins using the unspecific proteinase K under defined conditions. The proteinase k preferentially cleaves unfolded accessible regions, resulting in limited proteolysis. Following the LiP reaction all proteins are denatured and digested with trypsin.The resulting peptides can be quantified using several mass spectrometric technologies including MRMPRM, DDA and HRM (DIA). HRM is particularly suitable as an analytical platform for LiP since it allows the acquisition of all detectable peptide signals in a comprehensive HRM digital map.

Developed by the group of Prof. Paola Picotti at ETH Zurich, this patented technology (WO2014082733 A1) is exclusively licensed to Biognosys. Biognosys is currently developing applications of the LiP technology such as the identification of small molecule binding sites (e.g. for drug target deconvolution) and proteome-wide discovery of induced structural changes. Biognosys plans to commercialize the technology as a contract research services later this year.

We encourage you to read more on the LiP technology in the recent papers by the Picotti group:
• “Cell-wide analysis of protein thermal unfolding reveals determinants of thermostability” published in Science 
• “Global analysis of protein structural changes in complex proteomes” published in Nature Biotechnology

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