5969-19-7Relevant academic research and scientific papers
Modified coumarins. 9. Synthesis of amino-acid derivatives of 3-(2,3,5-trimethyl-7-oxofuro-[3,2-g]chromen-6-YL)propanoic acid
Veselovskaya,Shilin,Garazd,Khilya
, p. 177 - 181 (2003)
Furocoumarins modified by amino acids were prepared by condensation of the N-hydroxysuccinimide ester of 3-(2,3,5-trimethyl-7-oxofuro[3,2-g]chromen-6-yl) propanoic acid with amino acids.
Novel furocoumarins as potential HIV-1 integrase inhibitors
Olomola, Temitope O.,Mosebi, Salerwe,Klein, Rosalyn,Traut-Johnstone, Telisha,Coates, Judy,Hewer, Raymond,Kaye, Perry T.
, p. 1 - 4 (2014)
A series of seven novel, rationally designed N-substituted 3-{3,5-dimethylfuro[3,2-g]coumarin-6-yl}propanamides have been prepared as potential HIV-1 integrase (IN) inhibitors via a five-step pathway commencing with resorcinol and diethyl 2-acetylglutarate, and the HIV-1 IN inhibition potential of these compounds has been examined relative to raltegravir, a known HIV-1 IN inhibitor.
A focused structure-activity relationship study of psoralen-based immunoproteasome inhibitors
?terman, Andrej,Gobec, Martina,Gobec, Stanislav,Mravljak, Janez,Ra??an, Irena Mlinari?,Schiffrer, Eva Shannon,Sosi?, Izidor
, p. 1958 - 1965 (2019/11/20)
The immunoproteasome is a multicatalytic protease that is predominantly expressed in cells of hematopoietic origin. Its elevated expression has been associated with autoimmune diseases, various types of cancer, and inflammatory diseases. The development of immunoproteasome-selective inhibitors with non-peptidic scaffolds remains a challenging task. Here, we describe a focused series of psoralen-based inhibitors of the β5i subunit of the immunoproteasome with different substituents placed at position 4′. The most promising compound was further evaluated through changes at position 3 of the psoralen ring. Despite a small decrease in the inhibitory potency in comparison with the parent compound, we were able to improve the selectivity against other subunits of both the immunoproteasome and the constitutive proteasome. The most potent compounds discriminated between both proteasome types in cell lysates and also showed a decrease in cytokine secretion in peripheral blood mononuclear cells.
An AKAP-Lbc-RhoA interaction inhibitor promotes the translocation of aquaporin-2 to the plasma membrane of renal collecting duct principal cells
Schrade, Katharina,Tr?ger, Jessica,Eldahshan, Adeeb,Zühlke, Kerstin,Abdul Azeez, Kamal R.,Elkins, Jonathan M.,Neuenschwander, Martin,Oder, Andreas,Elkewedi, Mohamed,Jaksch, Sarah,Andrae, Karsten,Li, Jinliang,Fernandes, Joao,Müller, Paul Markus,Grunwald, Stephan,Marino, Stephen F.,Vuki?evi?, Tanja,Eichhorst, Jenny,Wiesner, Burkhard,Weber, Marcus,Kapiloff, Michael,Rocks, Oliver,Daumke, Oliver,Wieland, Thomas,Knapp, Stefan,Von Kries, Jens Peter,Klussmann, Enno
, (2018/02/06)
Stimulation of renal collecting duct principal cells with antidiuretic hormone (arginine-vasopressin, AVP) results in inhibition of the small GTPase RhoA and the enrichment of the water channel aquaporin-2 (AQP2) in the plasma membrane. The membrane inser
Nonpeptidic Selective Inhibitors of the Chymotrypsin-Like (β5 i) Subunit of the Immunoproteasome
Sosi?, Izidor,Gobec, Martina,Brus, Boris,Knez, Damijan,?ivec, Matej,Konc, Janez,Le?nik, Samo,Ogrizek, Mitja,Obreza, Ale?,?igon, Du?an,Jane?i?, Du?anka,Mlinari?-Ra??an, Irena,Gobec, Stanislav
supporting information, p. 5745 - 5748 (2016/05/09)
Elevated expression of the immunoproteasome has been associated with autoimmune diseases, inflammatory diseases, and various types of cancer. Selective inhibitors of the immunoproteasome are not only scarce, but also almost entirely restricted to peptide-based compounds. Herein, we describe nonpeptidic reversible inhibitors that selectively block the chymotrypsin-like (β5i) subunit of the human immunoproteasome in the low micromolar range. The most potent of the reversibly acting compounds were then converted into covalent, irreversible, nonpeptidic inhibitors that retained selectivity for the β5i subunit. In addition, these inhibitors discriminate between the immunoproteasome and the constitutive proteasome in cell-based assays. Along with their lack of cytotoxicity, these data point to these nonpeptidic compounds being suitable for further investigation as β5i-selective probes for possible application in noncancer diseases related to the immunoproteasome.
PSORALEN DERIVATIVES AS NON-PEPTIDIC INHIBITORS OF CHYMOTRYPSIN-LIKE ACTIVITY OF THE IMMUNOPROTEASOME
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Paragraph 0042; 0043; 0044; 0045, (2016/10/11)
This invention relates to new inhibitors of chymothrypsin-like activity of the immunoproteasome (inhibitors of β5? or LMP7 subunit) with the general formula (I), where substituents are described in patent description. Compounds can be in the form of pure enantiomers or as racemic mixtures, or in the form of pharmaceutically acceptable salts. The present invention relates to the use of these inhibitors for the treatment of diseases where immunoproteasome activity is increased.
Syntheses on the basis of 2H-chromen-2-one and 2H-chromene-2-thione
Avetisyan,Alvandzhyan
, p. 1063 - 1067 (2007/10/03)
4-Hydroxy-2H-chromen-2-one and 4-hydroxy-2H-chromene-2-thione reacted with allyl bromide, 1,1,3-trichloroprop-1-ene, and 1,3-dichlorobut-2-ene to give the corresponding ethers, which were oxidized to (2-oxo-2H-chromen-4-yloxy)acetic acid with potassium permanganate, and various derivatives of that acid were obtained. 3-(3,3-Dichloroprop-2-enyl)-7-hydroxy-4-methyl-2H-chromen-2-one and 3-(3,3-dichloroprop-2-enyl)-7-hydroxy-4-methyl-2H-chromene-2-thione were synthesized, and some their transformations were studied. Pleiades Publishing, Inc., 2006.
Synthesis of modified psoralen analogues
Garazd,Garazd,Ogorodniichuk,Khilya
, p. 291 - 300 (2007/10/03)
Substituted 3-(5-methyl-7-oxofuro[3,2-g]chromen-6-yl)propanoic acids analogous to psoralen were synthesized by linear annulation of a furan moiety to the coumarin system.
