692764-89-9

Basic information

• Product Name: 5-(4-Methoxy[1,1'-biphenyl]-3-yl)-1,2,5-thiadiazolidin-3-one 1,1-dioxide
• Synonyms: 5-(4-Methoxy[1,1'-biphenyl]-3-yl)-1,2,5-thiadiazolidin-3-one 1,1-dioxide;1,2,5-Thiadiazolidin-3-one, 5-(4-Methoxy[1,1'-biphenyl]-3-yl)-, 1,1-dioxide;5-(2-methoxy-5-phenylphenyl)-1,1-dioxo-1,2,5-thiadiazolidin-3-one
• CAS NO: 692764-89-9
• Molecular Formula: C15H14N2O4S
• Molecular Weight: 318
• Mol File: 692764-89-9.mol
• Article Data: 3

Chemical Properties

• Appearance: /
• Density: 1.370
• CAS DataBase Reference: 5-(4-Methoxy[1,1'-biphenyl]-3-yl)-1,2,5-thiadiazolidin-3-one 1,1-dioxide(CAS DataBase Reference)
• NIST Chemistry Reference: 5-(4-Methoxy[1,1'-biphenyl]-3-yl)-1,2,5-thiadiazolidin-3-one 1,1-dioxide(692764-89-9)
• EPA Substance Registry System: 5-(4-Methoxy[1,1'-biphenyl]-3-yl)-1,2,5-thiadiazolidin-3-one 1,1-dioxide(692764-89-9)

Safety Data

• Hazardous Substances Data: 692764-89-9(Hazardous Substances Data)

Upstream product

• 692765-84-7 5-(5-bromo-2-methoxyphenyl)-1,2,5-thiadiazolidin-3-one 1,1-dioxide 
• 98-80-6 phenylboronic acid 
• 39811-17-1 5-phenyl-O-anisidine 
• 852835-46-2 (4-methoxy-biphenyl-3-ylamino)-acetic acid methyl ester 
• 852835-51-9 C₁₆H₁₈N₂O₅S 

Relevant articles and documents

Covalent Allosteric Inactivation of Protein Tyrosine Phosphatase 1B (PTP1B) by an Inhibitor-Electrophile Conjugate

Protein tyrosine phosphatase 1B (PTP1B) is a validated drug target, but it has proven difficult to develop medicinally useful, reversible inhibitors of this enzyme. Here we explored covalent strategies for the inactivation of PTP1B using a conjugate composed of an active site-directed 5-aryl-1,2,5-thiadiazolidin-3-one 1,1-dioxide inhibitor connected via a short linker to an electrophilic α-bromoacetamide moiety. Inhibitor-electrophile conjugate 5a caused time-dependent loss of PTP1B activity consistent with a covalent inactivation mechanism. The inactivation occurred with a second-order rate constant of (1.7 ± 0.3) × 102 M-1 min-1. Mass spectrometric analysis of the inactivated enzyme indicated that the primary site of modification was C121, a residue distant from the active site. Previous work provided evidence that covalent modification of the allosteric residue C121 can cause inactivation of PTP1B [Hansen, S. K., Cancilla, M. T., Shiau, T. P., Kung, J., Chen, T., and Erlanson, D. A. (2005) Biochemistry 44, 7704-7712]. Overall, our results are consistent with an unusual enzyme inactivation process in which noncovalent binding of the inhibitor-electrophile conjugate to the active site of PTP1B protects the nucleophilic catalytic C215 residue from covalent modification, thus allowing inactivation of the enzyme via selective modification of allosteric residue C121.

5- (SUBSTITUTED PHENYL) -THIADIAZOLIDINE-3-ONES AND THEIR USE AS PTP1B

The invention concerns compounds of the formula (I) or pharmaceutically acceptable salts thereof (A chemical formula should be inserted here - please see paper copy enclosed herewith) wherein R1, R2, R3, R4, R5, and R6 have any of the meanings defined in the description. Processes for the manufacture of compounds of formula (I), compositions containing them, their use as inhibitors of protein tyrosine phosphatase PTP1B and their use for the treatment of diabetes mellitus are also described.