244611-09-4

Basic information

• Product Name: 2,3-bis-O-tert-butyldimethylsilyl-5-O-triphenylmethyl-D-ribono-γ-lactone
• Synonyms: 2,3-bis-O-tert-butyldimethylsilyl-5-O-triphenylmethyl-D-ribono-γ-lactone
• CAS NO: 244611-09-4
• Molecular Weight: 618.961
• Mol File: 244611-09-4.mol

Chemical Properties

• CAS DataBase Reference: 2,3-bis-O-tert-butyldimethylsilyl-5-O-triphenylmethyl-D-ribono-γ-lactone(CAS DataBase Reference)
• NIST Chemistry Reference: 2,3-bis-O-tert-butyldimethylsilyl-5-O-triphenylmethyl-D-ribono-γ-lactone(244611-09-4)
• EPA Substance Registry System: 2,3-bis-O-tert-butyldimethylsilyl-5-O-triphenylmethyl-D-ribono-γ-lactone(244611-09-4)

Safety Data

• Hazardous Substances Data: 244611-09-4(Hazardous Substances Data)

Upstream product

• 84911-43-3 (3R,4S,5R)-3,4-dihydroxy-5-(trityloxymethyl)-dihydrofuran-2(3H)-one 
• 18162-48-6 tert-butyldimethylsilyl chloride 
• 5336-08-3 D-Ribono-1,4-lactone 
• 76-83-5 trityl chloride 
• 69739-34-0 t-butyldimethylsiyl triflate 

Downstream Products

• 244611-11-8 2,3-bis-O-tert-butyldimethylsilyl-1,4-bis-O-methanesulfonyl-5-O-triphenylmethyl-D-ribitol 
• 244611-10-7 2,3-bis-O-tert-butyldimethylsilyl-5-O-triphenylmethyl-D-ribitol 

Relevant articles and documents

Synthesis of a protected 3,4-dihydroxyproline from a pentose sugar

Formula presented D-Ribonolactone (6) was transformed into N-((fluorenylmethoxy)carbonyl)-3,4.bis.O-(tert-butyldimethylsilyl)-D-2,3-cis-3, 4-cis-3,4-dihydroxyproline (13) in nine chemical steps. This represents a potentially general strategy for the synth

FLUORESCENT SUBSTRATES FOR POLY(ADP-RIBOSYL) HYDROLASES

The post-translational modification (PTM) and signaling molecule poly(ADP-ribose) (PAR) has an impact on diverse biological processes. PTM is regulated by a series of ADP-ribosyl glycohydrolases (PARG enzymes) that cleave polymers and/or liberate monomers from their protein targets. Disclosed herein is a substrate for monitoring PARG activity, TFMU-ADPr, which directly reports on total PAR hydrolase activity via release of a fluorophore; this substrate has excellent reactivity, generality, stability, and usability. A second substrate, TFMU-IDPr, selectively reports on PARG activity only from the enzyme ARH3. Use of these probes in whole-cell lysate experiments has revealed a mechanism by which ARH3 is inhibited by cholera toxin. TFMU-ADPr and TFMU-IDPr are versatile tools for assessing small-molecule inhibitors in vitro and probing the regulation of ADP-ribosyl catabolic enzymes.

Synthesis of Dimeric ADP-Ribose and Its Structure with Human Poly(ADP-ribose) Glycohydrolase

Poly(ADP-ribosyl)ation is a common post-translational modification that mediates a wide variety of cellular processes including DNA damage repair, chromatin regulation, transcription, and apoptosis. The difficulty associated with accessing poly(ADP-ribose) (PAR) in a homogeneous form has been an impediment to understanding the interactions of PAR with poly(ADP-ribose) glycohydrolase (PARG) and other binding proteins. Here we describe the chemical synthesis of the ADP-ribose dimer, and we use this compound to obtain the first human PARG substrate-enzyme cocrystal structure. Chemical synthesis of PAR is an attractive alternative to traditional enzymatic synthesis and fractionation, allowing access to products such as dimeric ADP-ribose, which has been detected but never isolated from natural sources. Additionally, we describe the synthesis of an alkynylated dimer and demonstrate that this compound can be used to synthesize PAR probes including biotin and fluorophore-labeled compounds. The fluorescently labeled ADP-ribose dimer was then utilized in a general fluorescence polarization-based PAR-protein binding assay. Finally, we use intermediates of our synthesis to access various PAR fragments, and evaluation of these compounds as substrates for PARG reveals the minimal features for substrate recognition and enzymatic cleavage. Homogeneous PAR oligomers and unnatural variants produced from chemical synthesis will allow for further detailed structural and biochemical studies on the interaction of PAR with its many protein binding partners. (Chemical Equation Presented).

Toward a general strategy for the synthesis of 3,4-dihydroxyprolines from pentose sugars

A general strategy is proposed, wherein a pentose sugar γ-lactone can be converted, via a series of nine reactions, to a 3,4-dihydroxyproline, suitably protected for use in peptide synthesis. Thus, D-ribonolactone (6) has been converted to N-fluorenylmethoxycarbonyl-3,4-di-O-tert-butyldimethylsilyloxy-D-2,3-cis-3, 4-cis-proline (7) in 18.9% overall yield. Likewise, L-arabinonolactone (11) has been converted to N-fluorenylmethoxycarbonyl-3,4-di-O-tert-butyldimethylsilyloxy-L-2,3-cis-3, 4-trans-proline (36) in 13.7% overall yield and L-lyxonolactone (12) to N-fluorenylmethoxycarbonyl- 3,4-di-O-tert-butyldimethylsilyloxy-L-2,3-trans-3,4-cis-proline (37) in 11.2% overall yield. These building blocks have also been fully deprotected to give the free amino acids. We believe that this series of reactions ought to be applicable to the synthesis of any of the eight stereoisomers of 3,4-dihydroxyproline, by judicious selection of the pentose starting material.

Total synthesis of a glyoxalase I inhibitor and its precursor, (-)-KD16-U1

A glyoxalase I inhibitor and (-)-KD16-U1 have been synthesized from D-ribonic acid γ-lactone through SnCl4-promoted cyclization of a phenylsulfonyl enol silyl ether and regioselective introduction of a hydroxymethyl group.