Small Molecule Drug Targets Identification Service | ABPP

    Small molecule drugs play a very important role in the treatment of diseases, and their mechanism of action is to exert their function by interacting with specific target molecules in cells. These target molecules are mainly proteins, including enzymes, ion channel proteins, and other types. Therefore, the identification of the target protein of small molecule drug action is crucial for understanding the mechanism of action and application of small molecule drugs, and can also further discover the off-target targets, side effects, and biological functions involved in the target protein of small molecule drugs.


    Traditional methods for identifying drug targets use chemical modification-based approaches and label-free target identification methods. Chemical modification methods include affinity chromatography, active site-directed probe techniques, and protein microarray technologies among others. There are certain limitations to chemical modification-based methods, as they all require labeling or derivation of small molecule drugs or protein libraries, while small molecule drugs may lack sites for covalent cross-linking, or chemical modification may affect the binding between drugs and target proteins. Label-free target identification methods do not involve any chemical modification of small molecule drugs and can complement methods based on chemical modification. Many studies have applied label-free methods, including cellular thermal shift assay (CETSA), thermal proteome profiling (TPP), pulse proteolysis (PP), stability of proteins from rates of oxidation (SPROX), drug affinity responsive target stability (DARTS), limited proteolysis coupled to mass spectrometry (LiP-MS), and solvent-induced protein precipitation (SIP), which can identify multiple targets of small molecule drugs simultaneously.


    MtoZ Biolabs boasts a comprehensive analytical platform for small molecule drug targets, featuring an array of high-resolution mass spectrometers and auxiliary equipment like high-performance liquid chromatography. This platform is equipped with extensive data storage, retrieval, and analysis capabilities. The services offered by the platform include extraction of proteins from various sources, incubation of drugs with purified protein/cell/tissue samples, sample pre-treatment for mass spectrometry, sample fractionation by high-performance liquid chromatography, and mass spectrometry data collection, enabling identification and quantitative research of small molecule drug targets. The team can explore the best experimental conditions through multiple gradient experiments, collect data through mass spectrometry, and analyze detailed information on drug targets through bioinformatics analysis. MtoZ Biolabs can provide services such as protein expression, protein extraction, drug treatment, sample preparation, mass spectrometry data collection, and experimental data analysis, offering a one-stop solution for the identification and verification of small molecule drug targets.

  • • Activity-Based Protein Profiling (ABPP) Service

    Activity-based protein profiling (ABPP) is a versatile and powerful chemoproteomic technique, utilizing activity-based probes (ABPs) that selectively and covalently interact with the active sites of proteins. This approach allows for the capture and analysis of tagged proteins using various proteomic tools. ABPP facilitates the global and quantitative examination of protein functional states in complex biological systems, including intact cells and animal models.  

  • • Drug Affinity Responsive Target Stability Analysis Service

    Drug affinity responsive target stability is a label-free small molecule probe technique under chemical proteomics first proposed by Lomenick et al. in 2009, which makes it possible to track and identify target proteins whose stability changes after binding with small molecules. To date, Drug affinity responsive target stability has been a focus in tracking proteins in animals, fungi, bacteria, and plants, and is widely applied with high simplicity, efficiency, universality, and accuracy.

  • • Thermal Proteome Profiling (TPP) Service

    Thermal proteome profiling is a combination of cellular thermal shift assay and mass spectrometry, so it is also called MS-CETSA. Thermal proteomic profiling determines the stability of the entire proteome by measuring the amount of soluble protein in cells or cell lysates at different heating temperatures.

  • • Stability of Proteins From Rates of Oxidation Analysis Service

    To explore the local conformational function of proteins in relation to their native structural stability, Fitzgerald et al. developed a technique that utilized amide H/D exchange rates to detect protein amide groups. In this technique, the thermodynamic stability of proteins and protein ligand complexes was assessed by measuring the amide H/D exchange rate. This approach was later refined and evolved into the SPROX technology.

  • • Protein Structures and Interactions Analysis Service | Lip-MS

    Limited proteolysis mass spectrometry (LiP-MS) has some of the same mechanisms as DARTS. LiP-MS is a newly developed proteomics approach that combines finite protein breakdown with targeted proteomics workflows. LiP-MS analysis of biological samples under native conditions and limited proteolysis requires protein digestion with proteinase K and trypsin.

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