138433-75-7

Upstream product

• 138433-69-9 5-O-(tert-butyldiphenylsilyl)-3-O-benzyl-2-deoxy-D-ribonolactone 
• 58479-61-1 tert-butylchlorodiphenylsilane 
• 34371-14-7 2-deoxy-D-ribonolactone 
• 128111-92-2 (2S,3R)-2-<3,4-O-isopropylidene-2,3,4-trihydroxybut-1-yl>-1,3-dithiane 
• 128161-77-3 (2S,3R)-2-<2-O-benzyl-3,4-O-isopropylidene-2,3,4-trihydroxybut-1-yl>-1,3-dithiane 
• 138433-57-5 (2S,3R)-2-<2-O-benzyl-4-O-(tert-butyldiphenylsilyl)-2,3,4-trihydroxybut-1-yl>-1,3-dithiane 
• 138433-61-1 (2R,3S)-4-benzyloxy-5-tert-butyldiphenylsilanyloxymethyl-2-hydroxytetrahydrofuran 
• 138433-53-1 (2S,3R)-2-(2-O-benzyl-2,3,4-trihydroxybut-1-yl)-1,3-dithiane 

Downstream Products

• 138433-83-7 5-O-(tert-butyldiphenylsilyl)-3-O-tetradecanoyl-2-deoxy-D-ribonolactone 

Relevant academic research and scientific papers

Stereoselective Allylstannane Addition for a Convergent Synthesis of a Complex Molecule

A convergent methodology with 13 lineal steps for the synthesis of phormidolides B and C macrocyclic core is described. Stereoselective formation of the tetrahydrofuran (THF) core was achieved using a stereocontrolled allylation reaction. The key step of the synthesis is a (Z)-1,5-anti stereoselective allylstannane addition where a new stereocenter and a trisubstituted double bond are formed simultaneously. Finally, Shiina macrolactonization conditions improved the yield of the final cyclization.

Conformationally constrained analogues of diacylglycerol. Interaction of γ-lactones with the phorbol ester receptor of protein kinase C

Four 2-deoxy-erythro-1,4-lactones in the D- and L-series and the four corresponding 2-deoxy-threo-1,4-lactones, bearing myristic acid acyl groups at either primary or secondary alcohol functions, were synthesized from L-ascorbic and D-isoascorbic acids. These eight pentonolactones which represent all possible isomers in this series were designed as rigid analogues of 1,2-diacylglycerol (DAG). The inhibition by these compounds of the binding of [3H] phorbol-12,13-dibutyrate to protein kinase C (PK-C) demonstrated the importance in this context of stereochemistry and particularly of the orientation of the fatty acid side chain. The most effective inhibitor (13d, Ki = 2.3 μM) has a fixed conformation which is presumed to be similar to the conformation adopted by DAG when binding to PK-C. A three-point attachment model which has been previously used to rationalize the similar behavior of DAG and phorbol esters was extended to include additional points of equivalence between these two PK-C agonists. This extended model addresses the disposition of the lipophilic myristic acid side chain and the orientation of the lactone carbonyl group which functions as a hydrogen bond acceptor. In this new model, the most active isomer 13d provides the best fit of the eight pentonolactones to phorbol myristate acetate.