Background Information
Thermal Proteome Profiling (TPP) is a technique that assesses protein stability by applying heat to living cells or lysates and analyzing the resulting changes using mass spectrometry. By monitoring how proteins denature and precipitate at specific melting temperatures (Tm), TPP helps identify how drugs, ligands, or environmental factors influence the proteome. When a drug or ligand binds to a protein, it can alter the Tm, enabling detection of drug-target interactions. This approach is widely used in drug discovery and proteomics to study protein stability, interactions, and post-translational modifications.
Technical Platform
Our Advantages
1. No need to modify the target small molecules, avoid changes in structure-activity relationships, and simplify experimental design.
2. Applicable to pure proteins, Iysates (cells or tissues, etc.)
3. Reflect direct interactions between proteins and small molecules.
Case Study
Project Aim: Verify whether the target small molecule is directly bound to the target protein in cell lysate through TPP.
Solutions: Analyze the thermal stability of the target protein using Western blotting (Figure 1), temperature range TPP-TR (Figure 2)and compound concentration range TPP-CCR (Figure 3).
