Rapid Communication - Journal of Systems Biology & Proteome Research (2022) Volume 3, Issue 6

PROTEOME INTEGRAL SOLUBILITY ALTERATION ASSAY SENSITIVITY

In cell lysates, living cells, and organisms, a variety of substances, including medicines and monomolecular stimuli, change the physicochemical properties of proteins. These changes can be detected by adjusting the application of a component that affects stability and solubility, such as increased temperature. Drug concentration or agent intensity/concentration can be employed as a second dimension of variation. The Proteome Integral Solubility Alteration (PISA) assay significantly increases the analysis throughput for an unlimited number of factor variation points as compared to conventional methods, which fit curves to protein solubility data collected at various temperatures and drug doses. The PISA technique will likely be widely used in chemical biology and drug development. The idea behind thermal proteome profiling (TPP) is that proteins denature and become insoluble when heated. When proteins interact with tiny molecules (such medicines or metabolites), nucleic acids, or other proteins, as well as when they undergo posttranslational modifications, their thermal stability may change. TPP tracks the melting profile of hundreds of expressed proteins using multiplexed quantitative mass spectrometry-based proteomics. It's significant that this method can be applied in vitro, in situ, or in vivo. It has been successfully used to investigate protein-protein and protein-metabolite interactions as well as drug targets and off targets. In order to research fundamental biological processes and their underlying mechanisms, TPP offers a unique perspective on protein state and interactions in their natural context and at a proteome-wide level.

Author(s): Sudhansu Sekhar Patra

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