174213-76-4

Usage

Uses

Used in Pharmaceutical Industry:
(S)-2-(phenoxymethyl)pyrrolidine is used as a building block for the synthesis of various pharmaceutical compounds due to its unique structure and the presence of both a basic nitrogen atom and a phenol group, which can contribute to the biological activity of the resulting molecules.
Used in Agrochemical Industry:
(S)-2-(phenoxymethyl)pyrrolidine is used as a precursor in the development of agrochemicals, such as pesticides and herbicides, owing to its potential to enhance the biological activity and selectivity of these compounds through its structural features.

InChI:InChI=1/C11H15NO/c1-2-6-11(7-3-1)13-9-10-5-4-8-12-10/h1-3,6-7,10,12H,4-5,8-9H2/t10-/m1/s1

Upstream product

• 76-05-1 trifluoroacetic acid 
• 174213-51-5 (S)-tert-butyl 2-(phenoxymethyl)pyrrolidine-1-carboxylate 
• 53912-80-4 (S)-N-benzylprolinol 
• 113304-84-0 N-benzyl-(S)-proline methyl ester 
• 86661-32-7 (S)-tert-butyl 2-((tosyloxy)methyl)pyrrolidine-1-carboxylate 
• 108-95-2 phenol 
• 15761-39-4 1-(tert-butoxycarbonyl)-L-proline 
• 23356-96-9 (S)-1-Pyrrolidin-2-yl-methanol 
• 69610-40-8 N-(tert-butoxycarbonyl)-L-prolinol 

Downstream Products

• 220510-28-1 (S)-1-Methyl-5-(2-phenoxymethyl-pyrrolidine-1-sulfonyl)-1H-indole-2,3-dione 
• 899818-37-2 (S)-1-(p-tert-butyldimethylsilyloxybenzyl)-5-[1-(2-phenoxymethylpyrrolidinyl)sulfonyl]isatin 
• 899818-41-8 (S)-1-[4-(2-bromoethoxy)-benzyl]-5-(2-phenoxymethyl-pyrrolidine-1-sulfonyl)-1H-indole-2,3-dione 
• 872254-19-8 (S)-1-(4-Hydroxybenzyl)-5-(2-phenoxymethyl-pyrrolidine-1-sulfonyl)-1H-indole-2,3-dione 
• 220509-98-8 5-(2-phenoxymethyl-pyrrolidine-1-sulfonyl)-1H-indole-2,3-dione 
• 220510-31-6 [2,3-dioxo-5-(2-phenoxymethyl-pyrrolidine-1-sulfonyl)-2,3-dihydro-indol-1-yl]-acetic acid tert-butyl ester 

Relevant academic research and scientific papers

Synthesis of Optically Active N -(4-Hydroxynon-2-enyl)pyrrolidines: Key Building Blocks in the Total Synthesis of Streptomyces coelicolor Butanolide 5 (SCB-5) and Virginiae Butanolide A (VB-A)

Starting from 5-methylhexanal and (S)-configured N -propargylprolinol ethers, coupling delivered N -(4-hydroxynon-2-ynyl)prolinol derivatives as mixtures of C4 diastereomers. Resolution of the epimers succeeded after introduction of an (R)-mandelic ester derivative and subsequent HPLC separation. Alternatively, suitable oxidation gave the corresponding alkynyl ketone. Midland reagent controlled diastereoselective reduction afforded a defined configured propargyl alcohol with high selectivity. LiAlH 4reduction and Mosher analyses of the allyl alcohols enabled structure elucidation. The suitably protected products are used as key intermediates in enantioselective Streptomyces γ-butyrolactone signaling molecule total syntheses.

Efficient synthesis, biological evaluation, and docking study of isatin based derivatives as caspase inhibitors

ABTRACT: In this paper, a new series of isatin-sulphonamide based derivatives were designed, synthesised and evaluated as caspase inhibitors. The compounds containing 1-(pyrrolidinyl)sulphonyl and 2-(phenoxymethyl)pyrrolidin-1-yl)sulphonyl substitution at C5 position of isatin core exhibited better results compared to unsubstituted derivatives. According to the results of caspase inhibitory activity, compound 20d showed moderate inhibitory activity against caspase-3 and ?7 in?vitro compared to Ac-DEVD-CHO (IC50 = 0.016 ± 0.002 μM). Among the studied compounds, some active inhibitors with IC50s in the range of 2.33–116.91 μM were identified. The activity of compound 20d was rationalised by the molecular modelling studies exhibiting the additional van der Waals interaction of N-phenylacetamide substitution along with efficacious T-shaped π-π and pi-cation interactions. The introduction of compound 20d with good caspase inhibitory activity will help researchers to find more potent agents.

AMIDO-THIOPHENE COMPOUNDS AND THEIR USE

The present invention pertains generally to the field of therapeutic compounds. More specifically the present invention pertains to certain amido-thiophene compounds that, inter alia, inhibit 11 β-hydroxysteroid dehydrogenase type 1 (11 β-HSD1 ). The present invention also pertains to pharmaceutical compositions comprising such compounds, and the use of such compounds and compositions, both in vitro and in vivo, to inhibit 11 β-hydroxysteroid dehydrogenase type 1; to treat disorders that are ameliorated by the inhibition of 11 β-hydroxysteroid dehydrogenase type 1; to treat the metabolic syndrome, which includes disorders such as type 2 diabetes and obesity, and associated disorders including insulin resistance, hypertension, lipid disorders and cardiovascular disorders such as ischaemic (coronary) heart disease; to treat CNS disorders such as mild cognitive impairment and early dementia, including Alzheimer's disease; etc.

Design, synthesis, and biological characterization of a caspase 3/7 selective isatin labeled with 2-[18f]fluoroethylazide

Imaging of programmed cell death (apoptosis) is important in the assessment of therapeutic response in oncology and for diagnosis in cardiac and neurodegenerative disorders. The executioner caspases 3 and 7 ultimately effect cellular death, thus providing

Synthesis, radiolabeling, and in vivo evaluation of an 18F-labeled isatin analog for imaging caspase-3 activation in apoptosis

A non-peptide-based isatin sulfonamide analog, WC-II-89, was synthesized and its inhibition toward recombinant human caspase-3 and other caspases was determined. This compound showed high potency for inhibiting caspase-3 and -7, and high selectivity again

5-Pyrrolidinylsulfonyl isatins as a potential tool for the molecular imaging of caspases in apoptosis

Caspases are the unique enzymes responsible for the execution of the cell death program and may represent an exclusive target for the specific molecular imaging of apoptosis in vivo. 5-Pyrrolidinylsulfonyl isatins represent potent nonpeptidyl caspase inhibitors that may be suitable for the development of caspase binding radioligands (CBRs). (S)-5-[1-(2-Methoxymethylpyrrolidinyl) sulfonyl]isatin (7) served as a lead compound for modification of its N-1-position. Corresponding pairs of N-1-substituted 2-methoxymethyl- and 2-phenoxymethylpyrrolidinyl derivatives were examined in vitro by biochemical caspase inhibition assays. All target compounds possess high in vitro caspase inhibition potencies in the nanomolar to subnanomolar range for caspase-3 (Ki = 0.2-56.1 nM). As shown for compound (S)-1-(4-(2-fluoroethoxy) benzyl)-5-[1-(2-methoxymethylpyrrolidinyl)sulfonyl]isatin (35), the class of N-1-substituted 5-pyrrolidinylsulfonyl isatins competitively inhibits caspase-3. All caspase inhibitors show selectivity for the effector caspases-3 and -7 in vitro. The 2-methoxymethylpyrrolidinyl versions of the isatins appear to possess superior caspase inhibition potencies in cellular apoptosis inhibition assays compared with the 2-phenoxymethylpyrrolidinyl inhibitors.

N-benzylisatin sulfonamide analogues as potent caspase-3 inhibitors: Synthesis, in vitro activity, and molecular modeling studies

A number of isatin sulfonamide analogues were prepared and their potencies for inhibiting caspase-1, -3, -6, -7, and -8 were evaluated in vitro. Several compounds displaying a nanomolar potency for inhibiting the executioner caspases, caspase-3 and caspas

Caspases and apoptosis

The present invention is to novel compounds of Formula (I), their pharmaceutical compositions, and to the novel inhibition of Caspases for use in the treatment of apoptosis, and disease states caused by excessive or inappropriate cell death.

Potent and selective nonpeptide inhibitors of caspases 3 and 7

5-Dialkylaminosulfonylisatins have been identified as potent, nonpeptide inhibitors of caspases 3 and 7. The most active compound within this series (34) inhibited caspases 3 and 7 in the 2-6 nM range and exhibited approximately 1000-fold selectivity for caspases 3 and 7 versus a panel of five other caspases (1, 2, 4, 6, and 8) and was at least 20-fold more selective versus caspase 9. Sequence alignments of the active site residues of the caspases strongly suggest that the basis of this selectivity is due to binding in the S2 subsite comprised of residues Tyr204, Trp206, and Phe256 which are unique to caspases 3 and 7. These compounds inhibit apoptosis in three cell-based models: human Jurkat T cells, human chondrocytes, and mouse bone marrow neutrophils.