200424-69-7

Upstream product

• 108-94-1 cyclohexanone 
• 105-53-3 diethyl malonate 
• 120-92-3 cyclopentanone 
• 41589-43-9 cyclohexylidene malonic acid diethyl ester 
• 78775-64-1 (1-Methylcyclohexyl)malonsaeure-diethylester 

Downstream Products

• 361442-45-7 benzyloxycarbonylamino-(1-methyl-cyclohexyl)-acetic acid ethyl ester 
• 361442-46-8 tert-butoxycarbonylamino-(1-methyl-cyclohexyl)-acetic acid ethyl ester 
• 361442-47-9 tert-butoxycarbonylamino-(1-methyl-cyclohexyl)-acetic acid 

Relevant academic research and scientific papers

Protected amino hydroxy adamantane carboxylic acid and process for its preparation

Dipeptidyl peptidase IV (DP 4) inhibiting compounds are provided. The provided compounds can be used for treating diabetes and related diseases, especially Type II diabetes, and other diseases as set out herein, employing such DP 4 inhibitor or a combination of such DP 4 inhibitor and one or more of another antidiabetic agent such as metformin, glyburide, troglitazone, pioglitazone, rosiglitazone and/or insulin and/or one or more of a hypolipidemic agent and/or anti-obesity agent and/or other therapeutic agent.

Synthesis of Novel Potent Dipeptidyl Peptidase IV Inhibitors with Enhanced Chemical Stability: Interplay between the N-Terminal Amino Acid Alkyl Side Chain and the Cyclopropyl Group of α -Aminoacyl-L-cis-4,5-methanoprolinenitrile-Based Inhibitors

A series of methanoprolinenitrile-containing dipeptide mimetics were synthesized and assayed as inhibitors of the N-terminal sequence-specific serine protease dipeptidyl peptidase IV (DPP-IV). The catalytic action of DPP-IV is the principle means of degradation of glucagon-like peptide-1, a key mediator of glucose-stimulated insulin secretion, and DPP-IV inhibition shows clinical benefit as a novel mechanism for treatment of type 2 diabetes. However, many of the reversible inhibitors to date suffer from chemical instability stemming from an amine to nitrile intramolecular cyclization. Installation of a cyclopropyl moiety at either the 3,4- or 4,5-position of traditional 2-cyanopyrrolidide proline mimetics led to compounds with potent inhibitory activity against the enzyme. Additionally, cis-4,5-methanoprolinenitriles with β-branching in the N-terminal amino acid provided enhanced chemical stability and high inhibitory potency. This class of inhibitors also exhibited the ability to suppress prandial glucose elevations after an oral glucose challenge in male Zucker rats.