78902-03-1

Basic information

• Product Name: 1-(S)-chloro-2-phenylethylboronic acid (1S,2S,3R,5S)-(+)-pinane-2,3-glycol ester
• Synonyms: 1-(S)-chloro-2-phenylethylboronic acid (1S,2S,3R,5S)-(+)-pinane-2,3-glycol ester
• CAS NO: 78902-03-1
• Molecular Weight: 318.651
• Mol File: 78902-03-1.mol
• Article Data: 12

Chemical Properties

• CAS DataBase Reference: 1-(S)-chloro-2-phenylethylboronic acid (1S,2S,3R,5S)-(+)-pinane-2,3-glycol ester(CAS DataBase Reference)
• NIST Chemistry Reference: 1-(S)-chloro-2-phenylethylboronic acid (1S,2S,3R,5S)-(+)-pinane-2,3-glycol ester(78902-03-1)
• EPA Substance Registry System: 1-(S)-chloro-2-phenylethylboronic acid (1S,2S,3R,5S)-(+)-pinane-2,3-glycol ester(78902-03-1)

Safety Data

• Hazardous Substances Data: 78902-03-1(Hazardous Substances Data)

Upstream product

• 1589-82-8 phenylmagnesium bromide 
• 87249-60-3 (3aS,4S,6S,7aR)-2-(dichloromethyl)-3a,5,5-trimethylhexahydro-4,6-methanobenzo[d][1,3,2]dioxaborole 
• 87100-28-5 pinacol benzylboronate 
• 100-39-0 benzyl bromide 
• 4463-42-7 benzyl boronic acid 
• 76110-78-6 (3aS,4S,6S,7aR)-3a,5,5-trimethyl-2-phenylhexahydro-4,6-methanobenzo[d][1,3,2]dioxaborole 
• 18680-27-8 pinanediol 
• 75-09-2 dichloromethane 
• 78922-83-5 (1-phenylmethyl)boronic acid (1S,2S,3R,5S)-(+)-2,3-pinanediol ester 

Downstream Products

• 78902-04-2 (+)-pinanediol (1R)-1-(N,N-bis(trimethylsilyl)amino)-2-phenylethaneboronate 
• 78902-05-3 (+)-pinanediol (R)-1-acetamido-2-phenylethane-1-boronate 
• 514820-49-6 (R)-2-phenyl-1-((3aS,4S,6S,7aR)-3a,5,5-trimethylhexahydro-4,6-methanobenzo[d][1,3,2]dioxaborol-2-yl)ethanamine 2,2,2-trifluoroacetate 
• 1440790-32-8 C₆₆H₉₁BN₆O₁₀ 
• 1440790-38-4 C₆₉H₉₆BN₇O₁₁ 
• 178455-03-3 (R)-2-phenyl-1-((3a5,45,65,7aR)-3a,5,5-trimethylhexahydro-4,6-methanobenzo[d][1,3,2]dioxaborol-2-yl)ethanamine hydrochloride 
• 186906-12-7 (R)-2-phenyl-1-((3aS,4S,6S,7aR)-3a,5,5-trimethylhexahydro-4,6-methanobenzo[d][1,3,2]dioxaborol-2-yl)ethan-1-amine 

Relevant articles and documents

Boronic acid derivatives

The present invention relates to boronic acid derivatives; the present invention provides compounds of formula (I) or pharmaceutically acceptable salts, solvates, polymorphs or isomers thereof, pharmaceutical compositions comprising these compounds, and u

Structure-Based Optimization and Discovery of M3258, a Specific Inhibitor of the Immunoproteasome Subunit LMP7 (β5i)

Proteasomes are broadly expressed key components of the ubiquitin-dependent protein degradation pathway containing catalytically active subunits (β1, β2, and β5). LMP7 (β5i) is a subunit of the immunoproteasome, an inducible isoform that is predominantly expressed in hematopoietic cells. Clinically effective pan-proteasome inhibitors for the treatment of multiple myeloma (MM) nonselectively target LMP7 and other subunits of the constitutive proteasome and immunoproteasome with comparable potency, which can limit the therapeutic applicability of these drugs. Here, we describe the discovery and structure-based hit optimization of novel amido boronic acids, which selectively inhibit LMP7 while sparing all other subunits. The exploitation of structural differences between the proteasome subunits culminated in the identification of the highly potent, exquisitely selective, and orally available LMP7 inhibitor 50 (M3258). Based on the strong antitumor activity observed with M3258 in MM models and a favorable preclinical data package, a phase I clinical trial was initiated in relapsed/refractory MM patients.

Structure-based development of (1-(3′-Mercaptopropanamido)methyl)boronic Acid Derived Broad-Spectrum, Dual-Action Inhibitors of Metallo- And Serine-β-lactamases

The emergence and spread of bacterial pathogens acquired metallo-β-lactamase (MBL) and serine-β-lactamase (SBL) medicated β-lactam resistance gives rise to an urgent need for the development of new dual-action MBL/SBL inhibitors. Application of a pharmacophore fusion strategy led to the identification of (2′S)-(1-(3′-mercapto-2′-methylpropanamido)methyl)boronic acid (MS01) as a new dual-action inhibitor, which manifests broad-spectrum inhibition to representative MBL/SBL enzymes, including the widespread VIM-2 and KPC-2. Guided by the VIM-2:MS01 and KPC-2:MS01 complex structures, further structural optimization yielded new, more potent dual-action inhibitors. Selectivity studies indicated that the inhibitors had no apparent inhibition to human angiotensin-converting enzyme-2 and showed selectivity across serine hydrolyases in E. coli and human HEK293T cells labeled by the activity-based probe TAMRA-FP. Moreover, the inhibitors displayed potentiation of meropenem efficacy against MBL- or SBL-positive clinical isolates without apparent cytotoxicity. This work will aid efforts to develop new types of clinically useful dual-action inhibitors targeting MBL/SBL enzymes.