1132709-14-8

Basic information

• Product Name: ((S)-3-Methyl-1-((S)-3-phenyl-2-(pyrazine-2-carboxaMido)propanaMido)butyl)boronic acid
• Synonyms: ((S)-3-Methyl-1-((S)-3-phenyl-2-(pyrazine-2-carboxaMido)propanaMido)butyl)boronic acid;Boronic acid, B-[(1S)-3-Methyl-1-[[(2S)-1-oxo-3-phenyl-2-[(2-pyrazinylcarbonyl)aMino]propyl]aMino]butyl]-;(1S,2S)-BortezoMib;N-(2-Pyrazinecarbonyl)-L-phenylalanine-D-leucine boronic anhydride;(1S,2S)-Bortezomib Impurity;Bortezomib Impurity 19;[(1S)-3-methyl-1-[[(2S)-1-oxo-3-phenyl-2[(pyrazinylcarbonyl) amino]propyl]amino]butyl] boronic acid;Bortezomib Impurity PS619
• CAS NO: 1132709-14-8
• Molecular Formula: C₁₉H₂₅BN₄O₄
• Molecular Weight: 384.2372
• Product Categories: Chiral Reagents, Boron Derivatives, Inhibitors, Pharmaceuticals, Intermediates & Fine Chemicals
• Mol File: 1132709-14-8.mol
• Article Data: 6

Chemical Properties

• Appearance: /
• CAS DataBase Reference: ((S)-3-Methyl-1-((S)-3-phenyl-2-(pyrazine-2-carboxaMido)propanaMido)butyl)boronic acid(CAS DataBase Reference)
• NIST Chemistry Reference: ((S)-3-Methyl-1-((S)-3-phenyl-2-(pyrazine-2-carboxaMido)propanaMido)butyl)boronic acid(1132709-14-8)
• EPA Substance Registry System: ((S)-3-Methyl-1-((S)-3-phenyl-2-(pyrazine-2-carboxaMido)propanaMido)butyl)boronic acid(1132709-14-8)

Safety Data

• Hazardous Substances Data: 1132709-14-8(Hazardous Substances Data)

Usage

Uses

(1S,2S)-Bortezomib is an isomer of Bortezomib (B675700), proteasome inhibitor. (1S,2S)-Bortezomib has been seen to inhibit serine proteases shown to lower cellular Aβ concentrations, associated with Alzheimer’s or hypertension.

Upstream product

• 114457-94-2 (S)-3-phenyl-2[(pyrazine-2-carbonyl)-amino]propionic acid 
• 98-97-5 2-pyrazylcarboxylic acid 
• 16874-17-2 L-phenylalanine tert-butyl ester 
• 1161-13-3 N-Cbz-L-Phe 
• 1422969-07-0 C₃₂H₄₃BN₂O₅ 
• 1446194-56-4 (S)-N-(1-(isopentylamino)-1-oxo-3-phenylpropan-2-yl)pyrazine-2-carboxamide 
• 98-80-6 phenylboronic acid 
• 107-85-7 1-amino-3-methylbutane 

Relevant articles and documents

Structure-Based Design of Selective LONP1 Inhibitors for Probing in Vitro Biology

LONP1 is an AAA+ protease that maintains mitochondrial homeostasis by removing damaged or misfolded proteins. Elevated activity and expression of LONP1 promotes cancer cell proliferation and resistance to apoptosis-inducing reagents. Despite the importance of LONP1 in human biology and disease, very few LONP1 inhibitors have been described in the literature. Herein, we report the development of selective boronic acid-based LONP1 inhibitors using structure-based drug design as well as the first structures of human LONP1 bound to various inhibitors. Our efforts led to several nanomolar LONP1 inhibitors with little to no activity against the 20S proteasome that serve as tool compounds to investigate LONP1 biology.

Further characterization of a putative serine protease contributing to the γ-secretase cleavage of β-amyloid precursor protein

The 3-alkoxy-7-amino-4-chloro-isocoumarins JLK-6 and JLK-2 have been shown to markedly reduce the production of Amyloid β-peptide (Aβ) by Amyloid-β Precursor Protein (APP) expressing HEK293 cells by affecting the γ-secretase cleavage of APP, with no effect on the cleavage of the Notch receptor. This suggested that these compounds do not directly inhibit the presenilin-dependent γ-secretase complex but more likely interfere with an upstream target involved in γ-secretase-associated pathway. The mechanism of action of these compounds is unknown and there are high fundamental and therapeutical interests to unravel their target. Isocoumarin compounds were previously shown to behave as potent mechanism-based irreversible inhibitors of serine proteases, suggesting that the JLK-directed target could belong to such enzyme family. To get further insight into structure-activity relationships and to develop more potent isocoumarin derivatives, we have synthesized and evaluated a series of isocoumarin analogues with modifications at positions 3, 4 and 7. In particular, the 7-amino group was substituted with either acyl, urethane, alkyl or aryl groups, which could represent additional interaction sites. Altogether, the results highlighted the essential integrity of the 3-alkoxy-7-amino-4-chloro-isocoumarin scaffold for Aβ-lowering activity and supported the involvement of a serine protease, or may be more generally, a serine hydrolase. The newly reported 7-N-alkyl series produced the most active compounds with an IC50 between 10 and 30 μM. Finally, we also explored peptide boronates, a series of reversible serine protease inhibitors, previously shown to also lower cellular Aβ production. The presented data suggested they could act on the same target or interfere with the same pathway as isocoumarins derivatives.

Anti-Claudin 3 Monoclonal Antibody and Treatment and Diagnosis of Cancer Using the Same

Monoclonal antibodies that bind specifically to Claudin 3 expressed on cell surface are provided. The antibodies of the present invention are useful for diagnosis of cancers that have enhanced expression of Claudin 3, such as ovarian cancer, prostate cancer, breast cancer, uterine cancer, liver cancer, lung cancer, pancreatic cancer, stomach cancer, bladder cancer, and colon cancer. The present invention provides monoclonal antibodies showing cytotoxic effects against cells of these cancers. Methods for inducing cell injury in Claudin 3-expressing cells and methods for suppressing proliferation of Claudin 3-expressing cells by contacting Claudin 3-expressing cells with a Claudin 3-binding antibody are disclosed. The present application also discloses methods for diagnosis or treatment of cancers.