936571-71-0

Upstream product

• 150-13-0 4-amino-benzoic acid 
• 152120-54-2 N,N'-bis( tert-butoxycarbonyl)-1H-pyrazole-1-carboxamidine 
• 207857-15-6 1,3-di(tert-butyloxycarbonyl)-2-(trifluoromethylsulfonyl)guanidine 
• 24424-99-5 di-tert-butyl dicarbonate 

Downstream Products

• 936571-72-1 2(S)-[2(S)-(4-guanidino-benzoylamino)-3-methyl-butyrylamino]-3-phenyl-propionic acid 
• 1208115-83-6 C₃₅H₄₆N₈O₅ 
• 1427752-38-2 N-(3-{4-[(4-carbamimidamidobenzoyl)oxy]phenyl}propanoyl)-L-aspartic acid 
• 1427752-84-8 4-[4-(benzyloxy)-4-oxobutyl]phenyl 4-[N',N''-bis(tert-butoxycarbonyl)carbamimidamido]benzoate 

Relevant academic research and scientific papers

DOUBLE-HEADED PROTEASE INHIBITOR

The present invention provides a compound that is highly safe and useful in the prevention, alleviation, and/or treatment of various diseases involving enteropeptidase inhibition and/or trypsin inhibition, a pharmaceutical composition containing the compo

SUBSTITUTED PYRROLIDINES AS FACTOR XIA INHIBITORS FOR THE TREATMENT THROMBOEMBOLIC DISEASES

The present invention provides compounds of the general formula (I), their salts and N-oxides, and solvates and prodrugs thereof (wherein the substituents are as defined in the description). The compounds of the general formula (I) are inhibitors of factor XIa, and are useful in the prevention of and/or therapy for thromboembolic diseases.

Structure-based design of residue 1 analogs of the direct thrombin inhibitor pentapeptide FM 19

Myocardial ischemia and other acute coronary syndromes are leading causes of death worldwide, and often result from a thrombus that blocks an atherosclerotic coronary artery. A key enzyme in thrombus formation is the serine protease thrombin, which is responsible for both the conversion of soluble fibrinogen into insoluble fibrin, as well as the activation of the GPCRs, PAR1 and PAR4, which stimulate platelet aggregation. Thus, thrombin is an attractive target for anticoagulant and antithrombotic therapy. Previous studies in our laboratory led to the development of lead compound FM 19 (d-Arg-Oic-Pro-d-Ala-Phe(p-Me)-NH2), which shows modest potency as a thrombin inhibitor. The recently determined X-ray structure of FM 19 in the active site of thrombin has revealed potential sites for modification to improve potency. This study reports replacements to the first residue (d-Arg 1) of FM 19, which seek to improve potency by removing the N-terminal amine to eliminate an adverse electrostatic interaction, and alterations to the length of the side chain to eliminate an unfavorable eclipsed conformation observed in the X-ray structure. This study produced two compounds, 1 and 9, with improved α-thrombin inhibition (IC50 values of 0.66 ± 0.20 μm and 0.57 ± 0.12 μm, respectively).

Modifications of the GSK3β substrate sequence to produce substrate-mimetic inhibitors of Akt as potential anti-cancer therapeutics

Amplification, overexpression, and elevated activation of Akt have been detected in many human malignancies making it an important target for cancer therapy. The Akt substrate-binding site offers a large number of potential interactions to an appropriatel