Phosphatase Screening Library
Phosphatases are enzymes that catalyze the dephosphorylation process by replacing a phosphate group in a substrate with a hydroxyl group from activation water. Protein phosphorylation is a key post-translational modification in the regulation of many cellular processes. Phosphatases and kinases help regulate protein phosphorylation homeostasis in cells. The role of phosphatases is the opposite of that of phosphorylases and kinases. They play an important role in signal transduction pathways and control a wide variety of cellular processes including cell cycle, proliferation and differentiation, metabolism, cell-cell interactions, etc. Based on substrate specificity and functional diversity, protein phosphatases can be divided into two superfamilies: protein serine/threonine phosphatases and protein tyrosine phosphatases. Ser/Thr phosphatases are metalloenzymes belonging to two major gene families called PPP (phosphoprotein phosphatases) and PPM (metal-dependent protein phosphatases), while protein tyrosine phosphatases (PTP) belong to a different class of enzymes that utilize a phosphocysteine phosphatase intermediate as part of their catalytic action.
BOC Sciences can design a novel phosphatase screening library to deliver about 2,700 potential phosphatase inhibitors for high-throughput screening (HTS).
Figure 1. Classical protein tyrosine phosphatase (PTP) family. (Hojin, L.; et al. 2015)
Phosphatase Screening Library Design
- Firstly, we have employed a 2D fingerprint similarity search against a reference set of compounds from multiple databases of bioactive molecules
- Then, small molecules with similar compounds involved in the reference database are searched by utilizing the MDL public key
- Finally, our teams use BOC Sciences internal filters to identify more than 2,100 drug-like screening compounds and 600 close analogs of known phosphatase binding agents
At BOC Sciences, the potency of the bioactive compounds have been confirmed for the following phosphatase-related targets:
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
Figure 2. Schematic representation of approaches to identify PTP function and substrate. (Hojin, L.; et al. 2015)
Phosphatase Screening Library Characteristics
- High diversity over the screening set: mean Tanimoto > 0.85
- Favorable physicochemical parameters and solubility requirements
- No PAINS or toxic substances/unwanted functions: filtered by strict ‘Ro5-like’ physicochemical and most stringent in-house structural filters
- Bioactivity and safety confirmed by preclinical studies and clinical trials
- Structural diversity, medicinal activity, and cellular penetration
- Structural document, IC50, and other chemical and biological data are provided
- All compounds are continually updated
- Compound cherry-picking service is provided
What We Deliver
- Delivered within 2 weeks in any customer-preferred format
- Powders, dry films or DMSO solutions formatted in vials, 96 or 384-well plates
- All compounds have a minimum purity of 90% assessed by 1H NMR and HPLC
- Analytical data is provided
BOC Sciences provides professional, rapid and high-quality services of Phosphatase Screening Library design at competitive prices for global customers. Personalized and customized services of Phosphatase Screening Library design can satisfy any innovative scientific study demands. Our clients have direct access to our staff and prompt feedback to their inquiries. If you are interested in our services, please contact us immediately!
Reference
- Hojin, L.; et al. Mining the function of protein tyrosine phosphatases in health and disease. Seminars in Cell & Developmental Biology. 2015. 37: 66-72.
