329317-98-8

Usage

Uses

Used in Pharmaceutical Industry:
PTP Inhibitor IV is used as a research tool for studying the role of PTPs in various cellular processes and diseases. It helps researchers understand the mechanisms by which PTPs regulate signal transduction and contribute to the development of new therapeutic strategies targeting these enzymes.
Used in Drug Discovery:
PTP Inhibitor IV is used as a lead compound in the development of new drugs targeting PTPs. By inhibiting the activity of these enzymes, it may have potential therapeutic applications in the treatment of various diseases, such as cancer, autoimmune disorders, and neurological conditions, where PTPs are implicated in their pathophysiology.
Used in Biochemical Research:
PTP Inhibitor IV is used as a reagent in biochemical assays to investigate the activity and function of PTPs. It can be employed in enzyme inhibition assays, binding studies, and other experimental setups to evaluate the potency and selectivity of the inhibitor against specific PTPs.

Biological Activity

ptp inhibitor iv is a protein tyrosine phosphatases (ptps) inhibitor.ptps are reported to be important in the regulation of various signal transduction processes. enzymes of this class are considered as potential therapeutic targets in the treatment of various diseases including inflammation, diabetes, as well as cancer. however, previously identified ptp inhibitors are peptide-based containing a highly charged component, which usually lack membrane permeability resulting in their limited utility in the inhibition of intracellular phosphatases.

in vitro

ptp inhibitor iv was identified as an uncharged, 1,4-di-substituted, phenyl-linked bis-trifluoromethylsulfonamido phosphate mimetic acting as a competitive, reversible, and active-site directed inhibitor. it was noticed that ptp inhibitor iv showed greatly increased potency not only on ptp1b but also on the phosphatases shp-2 and mu. moreover, the interaction of the second so2cf3 moiety in ptp inhibitor iv with conserved arg residue of ptp might explain the increased inhibitory potency towards other ptps in addition to ptp1b [1].

IC 50

1.8, 2.5, 8.4, 13, 20, 6.4, and 6.7 μm for shp-2, ptp1b, ptp-ε, ptp-meg-2, ptp-σ, ptp-β, and ptp-μ, respectively

references

[1] huang, p. ,ramphal, j.,wei, j., et al. structure-based design and discovery of novel inhibitors of protein tyrosine phosphatases. bioor.med.chem. 11, 1835-1849 (2003).

Upstream product

• 358-23-6 trifluoromethylsulfonic anhydride 
• 2716-10-1 4,4'-(2,2-(1,4-phenylene)bis(propane-2,2-diyl))dibenzeneamine 

Relevant academic research and scientific papers

Structure-based design and discovery of novel inhibitors of protein tyrosine phosphatases

Protein tyrosine phosphatases (PTPs) are important in the regulation of signal transduction processes. Certain enzymes of this class are considered as potential therapeutic targets in the treatment of a variety of diseases such as diabetes, inflammation, and cancer. However, many PTP inhibitors identified to date are peptide-based and contain a highly charged phosphate-mimicking component. These compounds usually lack membrane permeability and this limits their utility in the inhibition of intracellular phosphatases. In the present study, we have used structure-based design and modeling techniques to explore catalytic-site directed, reversible inhibitors of PTPs. Employing a non-charged phosphate mimic and non-peptidyl structural components, we have successfully designed and synthesized a novel series of trifluoromethyl sulfonyl and trifluoromethyl sulfonamido compounds as PTP inhibitors. This is the first time that an uncharged phosphate mimic is reported in the literature for general, reversible, and substrate-competitive inhibition of PTPs. It is an important discovery because the finding may provide a paradigm for the development of phosphatase inhibitors that enter cells and modify signal transduction.