2227-98-7

Usage

Uses

Used in Pharmaceutical Industry:
5H-Pyrrolo[3,2-d]pyrimidin-4-amine (9CI) is used as a lead compound for the development of new drugs, particularly for its potential as an inhibitor of kinases and other enzyme targets. Its derivatives are being investigated for their anticancer properties, offering a promising avenue for the treatment of various types of cancer.
Used in Antiviral Applications:
In the field of antiviral research, 5H-Pyrrolo[3,2-d]pyrimidin-4-amine (9CI) is utilized as a potential antiviral agent, with its derivatives being studied for their ability to combat viral infections, providing a new approach to managing viral diseases.
Used in Antimalarial Applications:
5H-Pyrrolo[3,2-d]pyrimidin-4-amine (9CI) is also used as a starting point for the development of antimalarial drugs, with its derivatives showing promise in the fight against malaria, a disease that continues to impact global health.
Used in Chemical Synthesis:
As a building block in chemical synthesis, 5H-Pyrrolo[3,2-d]pyrimidin-4-amine (9CI) is employed in the creation of other biologically active molecules, contributing to the advancement of pharmaceuticals and other chemical compounds with therapeutic potential.
Overall, 5H-Pyrrolo[3,2-d]pyrimidin-4-amine (9CI) is a multifaceted chemical compound with applications spanning across various industries, particularly in healthcare and pharmaceuticals, where its potential to contribute to the development of new treatments is being actively explored.

InChI:InChI:1S/C6H6N4/c7-6-5-4(1-2-8-5)9-3-10-6/h1-3,8H,(H2,7,9,10)

Upstream product

• 84905-80-6 4-Chloro-5H-pyrrolo[3,2-d]pyrimidine 
• 252932-48-2 3-amino-2-ethoxycarbonylpyrrole 
• 5655-01-6 9-deazahypoxanthine 
• 2320-75-4 ethyl 4-amino-5H-pyrrolo[3,2-d]pyrimidine-7-carboxylate 
• 1335287-29-0 1,4-anhydro-2-deoxy-3,5-O-(di-tert-butylsilylene)-1-(4-N-pivaloylamino-pyrrolo[3,2-d]pyrimidin-7-yl)-4-thio-D-erythro-pento-1-enitol 
• 1335287-28-9 4-pivaloylamino-7-iodo-3H,5H-pyrrolo[3,2-d]pyrimidine 
• 1335287-27-8 4-pivaloylamino-3H,5H-pyrrolo[3,2-d]pyrimidine 

Downstream Products

• 653592-04-2 (3R,4S)-1-((4-amino-5H-pyrrolo[3,2-d]pyrimidin-7-yl)methyl)-4-((methylthio)methyl)pyrrolidin-3-ol 
• 653592-04-2 (3S,4R)-1-[(9-deazaadenin-9-yl)methyl]-3-hydroxy-4-(methylthiomethyl)-pyrrolidine 

Relevant academic research and scientific papers

COMPOSITIONS AND METHODS FOR THERAPY OF PROSTATE CANCER USING DRUG COMBINATIONS TO TARGET POLYAMINE BIOSYNTHESIS AND RELATED PATHWAYS

Provided are compositions and methods for treating prostate conditions. The methods involve administering to an individual in need thereof a composition that contains i) an inhibitor of methionine salvage pathway in prostate of the individual and ii) a polyamine analogue. The methods are for use in individuals who have been diagnosed with, or are suspected of having or at risk for developing androgen sensitive prostate cancer (AS-CaP), or Castration recurrent CaP (CR-CaP), or benign prostate hyperplasia (BPH). The disclosure includes use of inhibitors of methylthioadenosine phosphorylase (MTAP), and a polyamine analog that upregulates polyamine catabolism by increasing spermidine/spermine Nl -acetyl transferase (SAT1) activity, such as methylthio-DADMe-Immucillin (MTDIA), andl),N(11)-bisethylnorspermine (BENSpm), respectively. Pharmaceutical formulations that contain a combination of the inhibitor of the methionine salvage pathway and a polyamine analogue are included, as are kits that contain such agents.

Tight binding enantiomers of pre-clinical drug candidates

MTDIA is a picomolar transition state analogue inhibitor of human methylthioadenosine phosphorylase and a femtomolar inhibitor of Escherichia coli methylthioadenosine nucleosidase. MTDIA has proven to be a non-toxic, orally available pre-clinical drug candidate with remarkable anti-tumour activity against a variety of human cancers in mouse xenografts. The structurally similar compound MTDIH is a potent inhibitor of human and malarial purine nucleoside phosphorylase (PNP) as well as the newly discovered enzyme, methylthioinosine phosphorylase, isolated from Pseudomonas aeruginosa. Since the enantiomers of some pharmaceuticals have revealed surprising biological activities, the enantiomers of MTDIH and MTDIA, compounds 1 and 2, respectively, were prepared and their enzyme binding properties studied. Despite binding less tightly to their target enzymes than their enantiomers compounds 1 and 2 are nanomolar inhibitors.

SALT AND POLYMORPHIC FORMS OF (3R,4S)-L-((4-AMINO-5H-PYRROLO[3,2-D]PYRIMIDIN-7-YL)METHYL)-4(METHYLTHIOMETHYL)PYRODIN-3-OL(MTDIA)

The invention relates to salt forms of (3R,4S)-1-((4-amino-5H-pyrrolo[3,2-d]pyrimidin-7-yl)methyl)-4-(methylthiomethyl)pyrrolidin-3-ol, as well as polymorphic forms of the salts. The invention further relates to processes for preparing the salt forms and to the use of the salt forms in the treatment of diseases and disorders where it is desirable to inhibit 5'-methylthioadenosine phosphorylase (MTAP).

An access to the β-anomer of 4′-thio-C-ribonucleosides: Hydroboration of 1-C-aryl- or 1-C-heteroaryl-4-thiofuranoid glycals and its regiochemical outcome

We have developed a novel method for the synthesis of the β-anomer of 4′-thio-C-ribonucleosides from 3,5-O-(di-tert-butylsilylene)-4- thiofuranoid glycal. Palladium-catalyzed coupling of 1-tributylstannyl-4- thiofuranoid glycal with iodobenzene or a heter

Structure-activity relationships of adenine and deazaadenine derivatives as ligands for adenine receptors, a new purinergic receptor family

Adenine derivatives bearing substituents in the 2-, N6-, 7-, 8-, and/or 9-position and a series of deazapurines were synthesized and investigated in [3H]adenine binding studies at the adenine receptor in rat brain cortical membrane preparations (rAde1R). Steep structure-activity relationships were observed. Substitution in the 8-position (amino, dimethylamino, piperidinyl, piperazinyl) or in the 9-position (2-morpholinoethyl) with basic residues or introduction of polar substituents at the 6-amino function (hydroxy, amino, acetyl) represented the best modifications. Functional evaluation of selected adenine derivatives in adenylate cyclase assays at 1321N1 astrocytoma cells stably expressing the rAde1R showed that all compounds investigated were agonists or partial agonists. A subset of compounds was additionally investigated in binding studies at human embryonic kidney (HEK293) cells, which also express a high-affinity adenine binding site. Structure-affinity relationships at the human cell line were similar to those at the rAde1R, but not identical. In particular, N 6-acetyladenine (25, Ki rat: 2.85 μM; Ki human: 0.515 μM) and 8-aminoadenine (33, Ki rat: 6.51 μM; Ki human: 0.0341 μM) were much more potent at the human as compared to the rat binding site. The new AdeR ligands may serve as lead structures and contribute to the elucidation of the functions of the adenine receptor family. 2009 American Chemical Society.

N-Arylmethyl substituted iminoribitol derivatives as inhibitors of a purine specific nucleoside hydrolase

A key enzyme within the purine salvage pathway of parasites, nucleoside hydrolase, is proposed as a good target for new antiparasitic drugs. We have developed N-arylmethyl-iminoribitol derivatives as a novel class of inhibitors against a purine specific nucleoside hydrolase from Trypanosoma vivax. Several of our inhibitors exhibited low nanomolar activity, with 1,4-dideoxy-1,4-imino-N-(8-quinolinyl)methyl-d-ribitol (UAMC-00115, Ki 10.8 nM), N-(9-deaza-adenin-9-yl)methyl-1,4-dideoxy-1,4-imino-d-ribitol (Ki 4.1 nM), and N-(9-deazahypoxanthin-9-yl)methyl-1,4-dideoxy-1,4-imino-d-ribitol (Ki 4.4 nM) being the three most active compounds. Docking studies of the most active inhibitors revealed several important interactions with the enzyme. Among these interactions are aromatic stacking of the nucleobase mimic with two Trp-residues, and hydrogen bonds between the hydroxyl groups of the inhibitors and amino acid residues in the active site. During the course of these docking studies we also identified a strong interaction between the Asp40 residue from the enzyme and the inhibitor. This is an interaction which has not previously been considered as being important.