1046470-60-3

Upstream product

• 251444-03-8 (1R,2S)-2-(tert-butyldiphenylsilyloxy)methyl-1-formylcyclopropane 

Downstream Products

• 1046470-58-9 (1S,2S)-2-[(tert-butyldiphenylsiloxy)methyl]-1-[2-((R)-tert-butylsulfinyl)iminoethyl]cyclopropane 
• 1046470-56-7 (1S,2S)-2-[(tert-butyldiphenylsiloxy)methyl]-1-[2-((S)-tert-butylsulfinyl)iminoethyl]cyclopropane 
• 1355254-24-8 (2S,3S)-4-tert-butyldiphenylsilyloxy-2,3-methano-1-(1-triphenylmethyl-1H-imidazol-4-yl)butane 
• 1355254-31-7 (2S,3S)-4-formyl-2,3-methano-1-(1-triphenylmethyl-1H-imidazol-4-yl)butane 
• 1355254-38-4 (2S,3S)-4-(4-chlorobenzylamino)-2,3-methano-1-(1H-imidazol-4-yl)butane 
• 1447825-86-6 C₃₂H₃₉NO₄Si 
• 1447825-85-5 C₃₂H₃₉NO₄Si 
• 1447825-83-3 C₃₂H₃₉NO₄Si 

Relevant academic research and scientific papers

MACROCYCLIC INHIBITORS OF PEPTIDYLARGININE DEIMINASES

The present disclosure relates to novel compounds for use in therapeutic treatement of a disease associated with peptidylarginine deiminases (PADs), such as peptidylarginine deiminase type 4 (PAD4). The present disclosure also relates to processes and intermediates for the preparation of such compounds, methods of using such compounds and pharmaceutical compositions comprising the compounds described herein.

Investigation of the noncovalent binding mode of covalent proteasome inhibitors around the transition state by combined use of cyclopropylic strain-based conformational restriction and computational modeling

To develop potent covalent inhibitors, the noncovalent interactions around the transition state to form covalent bonding should be optimized because the potency of the inhibitor can be depending on the energy of the transition state. Here, we report an efficient analysis of the noncovalent binding mode of a potent covalent proteasome inhibitor 3a around the transition state by a combined use of the chemical approach, i.e., the cyclopropylic strain-based conformational restriction, and the computational docking approach. Furthermore, we calculated the binding energy of a series of salinosporamide derivatives in the predicted noncovalent complex around the transition state with the simulation model of proteasome constructed in this study, which was well correlated to their pIC50. Thus, the proposed docking methods to predict the noncovalent binding mode around the transition state of covalent inhibitors will be helpful toward the development of covalent inhibitors.

Cyclopropane-based stereochemical diversity-oriented conformational restriction strategy: Histamine H3 and/or H4 receptor ligands with the 2,3-methanobutane backbone

The stereochemical diversity-oriented conformational restriction strategy can be an efficient method for developing specific ligands for drug target proteins. To develop potent histamine H3 and/or H4 receptor ligands, a series of con

Synthesis of 2,3- and 3,4-methanoamino acid equivalents with stereochemical diversity and their conversion into the tripeptide proteasome inhibitor belactosin a and its highly potent cis-cyclopropane stereoisomer

(Chemical Equation Presented) A series of chiral 2,3- and 3,4-methanoamino acid equivalents of stereochemical diversity were designed and synthesized from our chiral cyclopropane units, using a diastereoselective Grignard addition with (R)- or (S)-t-butanesulfinyl imines as the key step. These equivalents were converted into the proteasome inhibitor belactosin A and its cis-cyclopropane stereoisomer. The unnatural cis-isomer was shown to be more than twice as potent as belactosin A as a proteasome inhibitor.