174740-41-1

Upstream product

• 1426661-52-0 N-[(3β)-3-(acetyloxy)-28-oxolup-20(29)-en-28-yl]-β-alanine 1-(1,1-dimethylethyl) ester 
• 472-15-1 Betulinic acid 
• 468742-68-9 3-[((1R,3aS,5aR,5bR,7aR,9S,11aR,11bR,13aR,13bR)-9-Acetoxy-1-isopropenyl-5a,5b,8,8,11a-pentamethyl-icosahydro-cyclopenta[a]chrysene-3a-carbonyl)-amino]-propionic acid methyl ester 
• 59868-82-5 3-O-acetylbetulinic acid chloride 
• 10376-50-8 3-O-acetylbetulinic acid 

Relevant academic research and scientific papers

Derivatives of 3-O-(3',3'-dimethylsuccinyl)-betulinic acid

The present invention relates to compounds of the following formula (I): or a pharmaceutically acceptable salt thereof, a stereoisomer or a mixture of stereoisomers in any proportion, in particular a mixture of enantiomers, and particularly a racemate mixture, in which R represents a (C1-C10)alkyl group substituted with one or more, preferably one or two, groups chosen from COOH and NHR1, with R1 representing a hydrogen atom or a -Alk, -C(O)-Alk or -C(O)O-Alk group, Alk representing a (C1-C6)alkyl group, as well as a method for preparing them, and their use as a medicine, notably for treating an infection with a retrovirus such as HIV.

Synthesis and biological evaluation of a new derivative of bevirimat that targets the Gag CA-SP1 cleavage site

Bevirimat (2), the first-in-class HIV-1 maturation inhibitor, shows a low efficacy due essentially to the natural polymorphism of its target, the CA-SP1 junction. Moreover, its low hydrosolubility makes it difficult to study its interaction with the CA-SP1 junction. We have synthesized new derivatives of bevirimat by adding different hydrophilic substituents at the C-28 position to improve their hydrosolubility and perform the structural study of a complex by NMR. Synthesis of the new derivatives, the effect of substituents at the C-28 position and their hydrosolubility are discussed. The ability of these molecules to inhibit viral infection and their cytotoxicity is assessed. Compared to the well-known bevirimat (2), one of our compounds (16) shows a higher hydrosolubility associated with a 2.5 fold increase in activity, a higher selectivity index and a better antiviral profile. Moreover, for the first time a direct interaction between a derivative of bevirimat (16) and the domain CA-SP1-NC is shown by NMR. Information from this study should allow us to decipher the mechanism by which bevirimat inhibits HIV-1 maturation and how the natural polymorphism of the spacer peptide SP1 triggers resistance to inhibitors.

Anti-AIDS agents 49. Synthesis, anti-HIV, and anti-fusion activities of IC9564 analogues based on betulinic acid

The betulinic acid derivative IC9564 inhibits human immunodeficiency virus (HIV)-1 entry. Among a series of IC9564 derivatives, 5 and 20 were the most promising compounds against HIV infection with EC50 values of 0.33 and 0.46 μM, respectively.

Betulinic acid derivatives: A new class of specific inhibitors of human immunodeficiency virus type 1 entry

A novel series of ω-aminoalkanoic acid derivatives of betulinic acid were synthesized and evaluated for their activity against human immunodeficiency virus (HIV). The anti-HIV-1 activity of several members of this new series was found to be in the nanomolar range in CEM 4 and MT-4 cell cultures. The optimization of the ω-aminoalkanoic acid side chain is described. The presence of an amide function within the side chain was found important for optimal activity. RPR 103611 (14g), a statine derivative, was found to be inactive against HIV-1 protease, reverse transcriptase, and integrase as well as on gp120/CD4 binding. 'Time of addition' experiments suggested interaction with an early step of HIV-1 replication. As syncytium formation, but not virus-cell binding, seems to be affected, betulinic acid derivatives are assumed to interact with the postbinding virus-cell fusion process.