35264-05-2

Usage

Uses

Used in Pharmaceutical Industry:
Tert-butoxycarbonylamino-cyclohexyl-acetic acid is used as a reactant for the synthesis of SCH 503034, an orally bioavailable NS3 protease inhibitor. This application is crucial in the development of antiviral drugs, particularly against hepatitis C virus (HCV). SCH 503034 targets the NS3 protease enzyme, which is essential for the virus's replication process, thereby inhibiting the viral life cycle and offering therapeutic benefits to patients suffering from HCV.

InChI:InChI=1/C13H23NO4/c1-13(2,3)18-12(17)14-10(11(15)16)9-7-5-4-6-8-9/h9-10H,4-8H2,1-3H3,(H,14,17)(H,15,16)

Upstream product

• 41034-52-0 1,2,3,4-tetrahydroisoquinoline-1-carboxylic acid 
• 24424-99-5 di-tert-butyl dicarbonate 
• 1070-19-5 N-(tert-butyloxycarbonyl) azide 
• 20763-30-8 D-2-amino-2-(1,4-cyclohexadien-1-yl)acetic acid 
• 124-38-9 carbon dioxide 
• 253426-70-9 tert-butyl cyclohexyl(phenylsulfonyl)methylcarbamate 
• 378784-00-0 rhodium 
• 2900-27-8 2-(tert-butoxycarbonylamino)-2-phenylacetic acid 
• 486-73-7 1-isoquinolinecarboxylic acid 

Downstream Products

• 140150-59-0 2-(tert-butoxycarbonyl(methyl)amino)-2-cyclohexylacetic acid 

Relevant academic research and scientific papers

Synthesis ofN-Boc-α-amino Acids from Carbon Dioxide by Electrochemical Carboxylation ofN-Boc-α-aminosulfones

Electrochemical reduction ofN-Boc-α-aminosulfones in DMF using an undivided cell equipped with a Pt plate cathode and an Mg rod anode under atmospheric pressure of bubbling carbon dioxide through the solution under constant current conditions resulted in a reductive C-S bond cleavage with elimination of benzenesulfinate ion generating the corresponding anion species followed by fixation of carbon dioxide to give the correspondingN-Boc-α-amino acids in moderate to good yields.

Antithrombotic azacycloalkylalkanoyl peptides and pseudopeptides

The present invention relates to azacycloalkylalkanoyl peptides and pseudopeptides which inhibit platelet aggregation and thrombus formation thereby being useful in the prevention and treatment of thrombosis associated with disease states such as myocardial infarction, stroke, peripheral arterial disease, and disseminated intravascular coagulation, to methods for the prevention or treatment of thrombosis in a mammal in need of such therapy comprising the administration of a therapeutically effective amount of such compounds, and to pharmaceutical compositions comprising such compounds.

Highly selective tripeptide thrombin inhibitors

Tripeptide aldehydes such as Boc-D-Phe-Pro-Arg-H (5l) exhibit potent direct inhibition of thrombin. This distinction offers important insight for the design of more potent and selective serine protease inhibitors which may be useful pharmacological tools and hold promise for development of clinically useful agents. The structure-activity relationships (SAR) on a series of anticoagulant peptides with high selectivity for the enzyme thrombin are discussed. The SAR is centered on a series of di- and tripeptide arginine aldehydes based on the structure of 5l. The structural and conformational role of the amino acid residue in position 1 was investigated by substitution with conformationally restricted aromatic amino acids, aromatic acids, and a dipeptide isostere containing the ψ[CH2N] amide bond replacement. Many of these peptides demonstrate potent antithrombotic activity along with selectivity toward thrombin, determined by comparison of in vitro inhibitory effects on trypsin, plasmin, factor Xa, and tissue plasminogen activator. Compound 5f, D-1-Tiq-Pro-Arg-H · sulfate is highly active and the most selective tripeptide aldehyde inhibitor of thrombin reported to date.

Claudogenic-interceptive nonapeptides

Compounds of the formula: in which Y is L-Leu or L-(N-methyl)-Leu or a non-toxic acid addition salt thereof, are potent ovulation inducers and claudogenic-interceptive agents useful in preventing or terminating pregnancy in mammals.