905716-08-7

Upstream product

• 869569-89-1 C₂₅H₃₇NO₄Si 
• 58479-61-1 tert-butylchlorodiphenylsilane 
• 745011-75-0 (R)-2-((tert-butoxycarbonyl)amino)-4-hydroxybutanoic acid 
• 872983-22-7 (2R)-2-tert-butoxycarbamoyl-4-(tert-butyldiphenylsiloxy)butyric acid 
• 905716-01-0 [3-(tert-butyl-diphenyl-silanyloxy)-1-(methoxy-methyl-carbamoyl)-propyl]-carbamic acid tert-butyl ester 

Downstream Products

• 872983-24-9 {(1R)-1-[(benzothiazol-2-yl)(hydroxy)methyl]-3-(tert-butyldiphenylsiloxy)propyl}carbamic acid tert-butyl ester 
• 956247-38-4 C₂₆H₃₇NO₃Si 
• 872983-91-0 (1-{1-[1-(benzothiazole-2-carbonyl)-3-(tert-butyl-diphenyl-silanyloxy)-propylcarbamoyl]-2-phenyl-ethylcarbamoyl}-2-methyl-propyl)-carbamic acid tert-butyl ester 
• 872983-25-0 [(1S)-1-((1S)-1-{(1R)-1-[(benzothiazol-2-yl)(hydroxy)methyl]-3-(tert-butyldiphenylsiloxy)propyl}carbamoyl)-2-methylpropyl]carbamic acid tert-butyl ester 

Relevant academic research and scientific papers

A stereoselective total synthesis of (-)-andrachcinidine via an olefin cross-metathesis protocol

A stereoselective total synthesis of 1-(2S,6R)-6-[(2S)-2-hydroxypentyl]-hexahydro-2-pyridinylacetone, (-)-andrachcinidine is reported. The strategy utilizes olefin cross-metathesis and intramolecular SN2 cyclization as the key steps.

Engineering D-amino acid containing novel protease inhibitors using catalytic site architecture

The mechanism of proteolysis by serine proteases is a reasonably well-understood process. Typically, a histidine residue acting as a general base deprotonates the catalytic serine residue and the hydrolytic water molecule. We disclose here, the use of an