Abstract
This article profiles five newly drugs containing fluorine along with fragments of amino acids or their derivatives approved by the FDA in 2024. These pharmaceuticals include Voydeya® (danicopan), Ojemda® (tovorafenib), Itovebi® (inavolisib), Scemblix® (asciminib), and Revuforj® (revumenib). For each drug, we discuss the discovery, therapeutic areas of application, and detailed chemical synthesis.
References
Vickery H.B., Schmidt C.L.A. The history of the discovery of the amino acids. Chem. Rev. 1931. 9(2): 169–318.
doi: 10.1021/cr60033a001.
Luisi P.L. The Emergence of Life: From Chemical Origins to Synthetic Biology. Cambridge University Press. 2006.
doi: 10.1017/CBO9780511817540
Anfinsen C.B., Edsall J.T., Richards F.M. Advances in Protein Chemistry. New York: Academic Press. 1972.
Michal G., Schomburg D., eds. Biochemical Pathways: An Atlas of Biochemistry and Molecular Biology. 2nd Ed. Oxford: Wiley-Blackwell. 2012.
Genchi G. An overview on D-amino acids. Amino Acids. 2017. 49(9): 1521–1533.
doi: 10.1007/s00726-017-2459-5.
Wong J. T.-F. A Co-Evolution Theory of the Genetic Code. Proc. Nat. Acad. Sci. USA. 1975. 72(5): 1909–1912.
doi: 10.1073/pnas.72.5.1909.
Trifonov E.N. Consensus temporal order of amino acids and evolution of the triplet code. Gene. 2000. 261(1): 139–151.
doi: 10.1016/s0378-1119(00)00476-5.
Higgs P.G., Pudritz R.E. A thermodynamic basis for prebiotic amino acid synthesis and the nature of the first genetic code. Astrobiology. 2009. 9 (5): 483–90.
doi: 10.1089/ast.2008.0280.
Meierhenrich U. Amino acids and the asymmetry of life. Berlin: Springer. 2008.
doi: 10.1007/978-3-540-76886-9.
Hanessian S. Reflections on the total synthesis of natural products: Art, craft, logic, and the chiron approach. Pure Appl. Chem.1993. 65(6): 1189–1204.
doi: 10.1351/pac199365061189.
Blaser H.U. The chiral pool as a source of enantioselective catalysts and auxiliaries. Chem. Rev. 1992. 92(5): 935–952.
doi: 10.1021/cr00013a009.
Kitadai N., Maruyama S. Origins of building blocks of life: A review. Geosci. Front. 2018. 9(4): 1117–1153.
doi: 10.1016/j.gsf.2017.07.007.
Danchin A. From chemical metabolism to life: the origin of the genetic coding process. Beilstein J. Org. Chem. 2017. 13(1): 1119–1135. doi: 10.3762/bjoc.13.111.
Frenkel-Pinter M., Samanta M., Ashkenasy G., Leman L.J. Prebiotic Peptides: Molecular Hubs in the Origin of Life. Chem. Rev. 2020. 120(11): 4707–4765.
doi: 10.1021/acs.chemrev.9b00664.
Milner-White E.J. Protein three-dimensional structures at the origin of life. Interface Focus. 2019. 9(6): 20190057.
doi: 10.1098/rsfs.2019.0057.
Chatterjee S., Yadav S. The Coevolution of Biomolecules and Prebiotic Information Systems in the Origin of Life: A Visualization Model for Assembling the First Gene. Life. 2022. 12(6): 834.
doi: 10.3390/life12060834.
Kirschning A. The coenzyme/protein pair and the molecular evolution of life. Nat. Prod. Rep. 2021. 38(5): 993–1010.
doi: 10.1039/D0NP00037J.
Gutteridge A., Thornton J.M. Understanding nature’s catalytic toolkit. Trends in Biochem. Sci. 2005. 30(11): 622–629.
doi: 10.1016/j.tibs.2005.09.006.
McCoy R.H., Meyer C.E., Rose W.C. Feeding experiments with mixtures of highly purified amino acids. VIII. Isolation and identification of a new essential amino acid.J. Biol. Chem. 1935. 112: 283–302.
Steinhardt J., Reynolds J. A. Multiple equilibria in proteins. New York: Academic Press. 1969.
Xie J., Schultz P.G. Adding amino acids to the genetic repertoire. Curr. Opin. Chem. Biol. 2005. 9(6): 548–554.
doi: 10.1016/j.cbpa.2005.10.011.
Park M.H. The post-translational synthesis of a polyamine-derived amino acid, hypusine, in the eukaryoti c translation initiation factor 5A (eIF5A). J. Biochem. 2006. 139(2): 161–169.
doi: 10.1093/jb/mvj034.
Curis E., Nicolis I., Moinard C. et al. Almost all about citrulline in mammals. Amino Acids. 2005. 29(3): 177–205.
doi: 10.1007/s00726-005-0235-4.
Sakami W., Harrington H. Amino acid metabolism. Annu. Rev. Biochem. 1963. 32(1): 355–398.
doi: 10.1146/annurev.bi.32.070163.002035.
Wang X., Li J., Dong G., Yue J. The endogenous substrates of brain CYP2D. Eur. J. Pharmacol. 2014. 724: 211–218.
doi: 10.1016/j.ejphar.2013.12.025.
Petroff O.A. GABA and glutamate in the human brain. Neurosci. 2002. 8(6): 562–573.
doi: 10.1177/1073858402238515.
Turner E.H., Loftis J.M., Blackwell A.D. Serotonin a la carte: supplementation with the serotonin precursor 5-hydroxytryptophan. Pharmacol. Ther. 2006. 109(3): 325–338.
doi: 10.1016/j.pharmthera.2005.06.004.
Kostrzewa R.M., Nowak P., Kostrzewa J.P. et al. Peculiarities of L-DOPA treatment of Parkinson’s disease. Amino Acids. 2005. 28(2): 157–164.
doi: 10.1007/s00726-005-0162-4.
Leuchtenberger W., Huthmacher K., Drauz K. Biotechnological production of amino acids and derivatives: current status and prospects. Appl. Microbiol. Biotechnol. 2005. 69(1): 1–8.
doi: 10.1007/s00253-005-0155-y.
Sanda F., Endo T. Syntheses and functions of polymers based on amino acids. Macromol. Chem. Phys. 1999. 200(12): 2651–2661.
doi: 10.1002/(SICI)1521-3935.
Lengyel P., Söll D. Mechanism of protein biosynthesis. Bacteriol. Rev. 1969. 33(2): 264–301.
doi: 10.1128/br.33.2.264-301.1969.
Marasco D., Perretta G., Sabatella M., Ruvo M. Past and future perspectives of synthetic peptide libraries. Curr. Protein Pept. Sci. 2008. 9(5): 447–467.
doi: 10.2174/138920308785915209.
Soloshonok V.A., Cai C., Hruby V.J., Meervelt L.V. Asymmetric synthesis of novel highly sterically constrained (2S,3S)-3-methyl-3-trifluoromethyl- and (2S,3S,4R)-3-trifluoromethyl-4-methylpyroglutamic acids. Tetrahedron. 1999. 55(41): 12045–12058.
doi: 10.1016/S0040-4020(99)00711-5.
Blaskovich M.A.T. Unusual amino acids in medicinal chemistry. J Med Chem. 2016. 59 (24): 10807–10836.
doi: 10.1021/acs.jmedchem.6b00319.
Han J., Konno H., Sato T. et al.Tailor-made amino acids in the design of small-molecule blockbuster drugs. Eur. J. Med. Chem. 2021. 220: 113448.
doi: 10.1016/j.ejmech.2021.113448.
Liu J., Han J., Izawa K. et al. Cyclic tailor-made amino acids in the design of modern pharmaceuticals. Eur. J. Med. Chem. 2020. 208: 112736.
doi: 10.1016/j.ejmech.2020.112736.
Stevenazzi A., Marchini M., Sandrone G., Vergani B., Lattanzio M. Amino acidic scaffolds bearing unnatural side chains: An old idea generates new and versatile tools for the life sciences. Bioorg. Med. Chem. Lett. 2014. 24(23): 5349–5356.
doi: 10.1016/j.bmcl.2014.10.016.
Ma J.S. Unnatural amino acids in drug discovery. Chim. Oggi-Chem. Today. 2003. 21(6): 65–68.
Liu A., Han J., Nakano A., et al. New pharmaceuticals approved by FDA in 2020: Small-molecule drugs derived from amino acids and related compounds. Chirality. 2022. 34(1): 86–103.
doi: 10.1002/chir.23376.
Han J., Lyutenko N.V., Sorochinsky A.E., et al. Tailor-Made Amino Acids in Pharmaceutical Industry: Synthetic Approaches to Aza-Tryptophan Derivatives. Chem. Eur. J. 2021. 27(70): 17510–17528.
doi: 10.1002/chem.202102485.
Yin Z., Hu W., Zhang W. et al. Tailor-made amino acid-derived pharmaceuticals approved by the FDA in 2019. Amino Acids. 2020. 52(9): 1227–1261.
doi: 10.1007/s00726-020-02887-4.
Hodgson D.R.W., Sanderson J.M. The synthesis of peptides and proteins containing non-natural amino acids. Chem. Soc. Rev. 2004. 33(7): 422–430.
doi: 10.1039/B312953P.
Henninot A., Collins J.C., Nuss J.M. The current state of peptide drug discovery: Back to the future? J. Med. Chem. 2018. 61(4): 1382–1414.
doi: 10.1021/acs.jmedchem.7b00318.
Han, J., Konno H., Sato T., et al. Peptidomimetics and Peptide-Based Blockbuster Drugs. Curr. Org. Chem. 2021. 25(14):1627–1658.
doi: 10.2174/1385272825666210610155047.
Qiu W., Gu X., Soloshonok, V.A. et al. Stereoselective synthesis of conformationally constrained reverse turn dipeptide mimetics. Tetrahedron Lett. 2001. 42(2): 145–148.
doi: 10.1016/S0040-4039(00)01864-5.
Fosgerau K., Hoffmann T. Peptide therapeutics: current status and future directions. Drug Discov. Today. 2015. 20(1): 122–128.
doi: 10.1016/j.drudis.2014.10.003.
Cai M., Cai C., Mayorov A.V. et al. Biological and conformational study of β-substituted prolines in MT-II template: steric effects leading to human MC5 receptor selectivity. J. Pept. Res. 2004. 63(2): 116–131.
doi: 10.1111/j.1399-3011.2003.00105.x.
Craik D.J., Fairlie D.P., Liras S., Price D. The future of peptide-based drugs. Chem. Biol. Drug Des. 2013. 81(1): 136–147.
doi: 10.1111/cbdd.12055.
Hamley I.W. Introduction to Peptide Science.Wiley: Weinheim, Germany. 2020.
ISBN: 978-1-119-69817-3.
Saladin K. Anatomy and Physiology: The Unity of Form and Function. 6th Ed. McGraw-Hill Science/Engineering/Math. 2011.
Soloshonok V.A., Izawa K. Eds. Asymmetric Synthesis and Application of α-Amino Acids. ACS Symposium Series 1009. Washington, District of Columbia: American Chemical Society, 2009.
Wang J., Sánchez-Roselló M., Aceña J.L. et al. Fluorine in pharmaceutical industry: Fluorine-containing drugs introduce ed to the market in the last decade (2001–2011). Chem. Rev. 2014. 114(4): 2432–2506.
doi: 10.1021/cr4002879.
Zhou Y., Wang J., Gu Z. et al. Next Generation of Fluorine-Containing Pharmaceuticals, Compounds Currently in Phase II–III Clinical Trials of Major Pharmaceutical Companies: New Structural Trends and Therapeutic Areas. Chem. Rev. 2016. 116(2): 422–518.
doi: 10.1021/acs.chemrev.5b00392.
Zhu Y., Han J.L., Wang J.et al. Modern Approaches for Asymmetric Construction of Carbon−Fluorine Quaternary Stereogenic Centers: Synthetic Challenges and Pharmaceutical Needs. Chem. Rev. 2018. 118(7): 3887−3964.
doi: 10.1021/acs.chemrev.7b00778.
Zhu W., Wang J., Wang S.et al.Recent advances in the trifluoromethylation methodology and new CF3-containing drugs. J. Fluorine Chem. 2014. 167: 37–54.
doi: 10.1016/j.jfluchem.2014.06.026.
Gillis E.P., Eastman K.J., Hill M.D. et al. Applications of Fluorine in Medicinal Chemistry. J. Med. Chem. 2015. 58(21): 8315–8359.
doi: 10.1021/acs.jmedchem.5b00258.
Meanwell N.A. Fluorine and Fluorinated Motifs in Design and Application of Bioisosteres for Drug Design. J. Med. Chem. 2018. 61(14): 5822–5880.
doi: 10.1021/acs.jmedchem.7b01788.
Johnson B.M., Shu Y-Z., Zhuo X., Meanwell N.A. Metabolic and Pharmaceutical Aspects of Fluorinated Compounds. J. Med. Chem. 2020. 63(12): 6315–86.
doi: 10.1021/acs.jmedchem.9b01877.
Han J., Kiss L., Mei H. et al. Chemical aspects of human and environmental overload with fluorine. Chem. Rev. 2021. 121(8): 4678–4742.
doi: 10.1021/acs.chemrev.0c01263.
Pan Y. The Dark Side of Fluorine. ACS Med. Chem. Lett. 2019. 10(7): 1016–1019.
doi: 10.1021/acsmedchemlett.9b00235.
Khan M.F., Murphy C.D. Bacterial degradation of the anti-depressant drug produces trifluoroacetic acid and fluoride ion. Appl. Microbiol. Biotechnol. 2021. 105(24): 9359–9369.
doi: 10.1007/s00253-021-11675-3.
Sun M., Cui J.N., Guo J. et al. Fluorochemicals biodegradation as a potential source of trifluoroacetic acid (TFA) to the environment. Chemosphere. 2020. 254: 126894.
doi: 10.1016/j.chemosphere.2020.126894.
Garnett K., Van Calster G. The Concept of Essential Use: A Novel Approach to Regulating Chemicals in the European Union. Transnatl. Environ. Law. 2021. 10(1): 159–187.
doi: 10.1017/S2047102521000042.
Mei H., Han J., Fustero S. Fluorine‐Containing Drugs Approved by the FDA in 2018. Chem. Eur. J. 2019. 25(51): 11797–11819.
doi: 10.1002/chem.201901840.
Han J., Remete A.M., Dobson L.S. et al. Next generation organofluorine containing blockbuster drugs. J. Fluor. Chem. 2020. 239: 109639.
doi: 10.1016/j.jfluchem.2020.109639.
Mei H., Remete A.M., Zou Y. et al. Fluorine-containing drugs approved by the FDA in 2019. Chin. Chem. Lett. 2020. 31(9): 2401–2413.
doi: 10.1016/j.cclet.2020.03.050.
He J., Li Z., Dhawan G. et al. Fluorine-containing drugs approved by the FDA in 2021. Chin. Chem. Lett. 2023. 34(1): 107578.
doi: 10.1016/j.cclet.2022.06.001.
Yu Y., Liu A., Dhawan G. et al. Fluorine-containing pharmaceuticals approved by the FDA in 2020: Synthesis and biological activity. Chin. Chem. Lett. 2021. 32(11): 3342–3354.
doi: 10.1016/j.cclet.2021.05.042.
Wang Q., Bian Y., Dhawan G. et al. FDA approved fluorine-containing drugs in 2023. Chin. Chem. Lett. 2024. 35(11): 109780.
doi: 10.1016/j.cclet.2024.109780.
Han J., Wzorek A., Dhawan G. et al. New drugs appearing on the market in 2023: molecules containing fluorine and fragments of tailor-made amino acids. Ukr. Bioorg. Acta. 2024. 19(1): 3–20.
Doi: 10.15407/bioorganica2024.01.003.
Wang N., Mei H., Dhawan G. et al. New Approved Drugs Appearing in the Pharmaceutical Market in 2022, Featuring Fragments of Tailor-Made Amino Acids and Fluorine. Molecules. 2023. 28(9): 3651.
doi: 10.3390/molecules28093651.
Li J., Zhou S., Wang J. et al.Asymmetric synthesis of aromatic and heteroaromatic α-amino acids using recyclable axially chiral ligand. Eur. J. Org. Chem. 2016. 2016(5): 999–1006.
doi: 10.1002/ejoc.201501442.
Mei H., Han J., White S. et al. Tailor-made amino acids and fluorinated motifs as prominent traits in modern pharmaceuticals. Chem. Eur. J. 2020. 26(50): 11349–11390.
doi: 10.1002/chem.202000617.
Mei H., Han J., Klika K.D. et al. Applications of fluorine-containing amino acids for drug design. Eur. J. Med. Chem. 2020. 186: 111826.
doi: 10.1016/j.ejmech.2019.111826.
Osipov S.N., Artyushin O.I., Kolomiets A.F. et al. Synthesis of fluorine‐containing cyclic α‐amino acid and α‐amino phosphonate derivatives by alkene metathesis. Eur. J. Org. Chem. 2001. 2001(20): 3891–3897.
doi:10.1002/1099-0690(200110)2001:20< 3891::AID-EJO C3891>3.0.CO;2-R.
Remete A.M., Nonn M., Fustero S. et al. Synthesis of fluorinated amino acid derivatives through late-stage deoxyfluorinations. Tetrahedron. 2018. 74(44): 6367–6418.
doi: 10.1016/j.tet.2018.09.021.
Konno T., Kanda M., Ishihara T., Yamanaka H. A novel synthesis of fluorine-containing quaternary amino acid derivatives via palladium-catalyzed allylation reaction. J. Fluorine Chem.2005. 126(11–12): 1517–1523.
doi: 10.1016/j.jfluchem.2005.08.013.
Krause H.W., Kreuzfeld H.J., Döbler C. Unusual amino acids: II. Asymmetric synthesis of fluorine containing phenylalanines. Tetrahedron: Asymmetry. 1992. 3(4): 555–566.
doi: 10.1016/S0957-4166(00)80262-1.
Tsushima T., Kawada K., Nishikawa J. et al. Fluorine-containing amino acids and their derivatives. 3. Stereoselective synthesis and unusual conformational features of threo- and erythro-3-fluorophenylalanine. J. Org. Chem. 1984. 49(7): 1163–1169.
doi: 10.1021/jo00181a003.
Vine W.H., Hsieh K.H., Marshall G.R. Synthesis of fluorine-containing peptides. Analogs of angiotensin II containing hexafluorovaline. J. Med. Chem.1981. 24(9): 1043–1047.
doi: 10.1021/jm00141a005.
Sorochinsky A.E., Ueki H., Aceña J.L. et al. Chemical deracemization and (S) to (R) interconversion of some fluorine-containing α-amino acids. J. Fluorine Chem. 2013. 152: 114–118.
doi: 10.1016/j.jfluchem.2013.02.022.
Smits R., Cadicamo C.D., Burger K., Koksch B. Synthetic strategies to α-trifluoromethyl and α-difluoromethyl substituted α-amino acids. Chem. Soc. Rev. 2008. 37(8): 1727–1739.
doi: 10.1039/B800310F.
Gutiérrez-Bonet Á., Liu W. Synthesis of alkyl fluorides and fluorinated unnatural amino acids via photochemical decarboxylation of α-fluorinated carboxylic acids. Org. Lett. 2023. 25(3): 483–487.
doi: 10.1021/acs.orglett.2c04144.
Soloshonok V. A., Cai C., Hruby V. J. et al. Stereochemically defined C-substituted glutamic acids and their derivatives. 1. An efficient asymmetric synthesis of (2S, 3S)-3-methyl- and -3-trifluoromethylpyroglutamic acids. Tetrahedron. 1999. 55(41): 12031–12044.
doi: 10.1016/S0040-4020(99)00711-5.
Soloshonok V.A., Avilov D.V., Kukhar V.P. Highly diastereoselective asymmetric aldol reactions of chiral Ni(II)-complex of glycine with alkyl trifluoromethyl ketones. Tetrahedron: Asymmetry. 1996. 7(6): 1547–1550.
doi: 10.1016/0957-4166(96)00177-2.
Soloshonok V.A., Kacharov A.D., Hayashi T. Gold(I)-catalyzed asymmetric aldol reactions of isocyanoacetic acid derivatives with fluoroaryl aldehydes. Tetrahedron. 1996. 52(1). 245–254.
doi: 10.1016/0040-4020(95)00893-D.
Soloshonok V.A., Kukhar V.P. Biomimetic base-catalyzed [1,3]-proton shift reaction. A practical synthesis of β-fluoroalkyl-β-amino acids. Tetrahedron. 1996. 52(20): 6953–6964.
doi: 10.1016/0040-4020(96)00300-6.
Soloshonok V.A., Hayashi T., Ishikawa K., Nagashima N. Highly diastereoselective aldol reaction of fluoroalkyl aryl ketones with methyl isocyanoacetate catalyzed by silver(I)/triethylamine. Tetrahedron Letters. 1994. 35(7): 1055–1058.
doi: 10.1016/S0040-4039(00)79964-3.
Soloshonok V.A., Avilov D.V., Kukhar V.P. et al. An efficient asymmetric synthesis of (2S, 3S)-3-trifluoromethylpyroglutamic acid. Tetrahedron Lett. 1997. 38(27): 4903–4904.
doi: 10.1016/S0040-4039(97)01054-X.
Soloshonok V.A., Kacharov A.D., Avilov D.V. et al. Transition metal/base-catalyzed aldol reactions of isocyanoacetic acid with prochiral ketones, a straightforward approach to stereochemically defined β,β-disubstituted-β-hydroxy-α-amino acids. Scope and limitations. J. Org. Chem. 1997. 62(11): 3470–3479.
doi: 10.1021/jo9623402.
Bravo P., Guidetti M., Viani F. et al. Chiral sulfoxide controlled asymmetric additions to C N double bond. An efficient approach to stereochemically defined α-fluoroalkyl amino compounds. Tetrahedron.1998. 54(42): 12789–12806.
doi: 10.1016/S0040-4020(98)00779-0.
Bravo P., Capelli S., Meille S.V. et al. Synthesis of optically pure (R)- and (S)-α-trifluoromethyl-alanine. Tetrahedron: Asymmetry. 1994. 5(10): 2009–2018.
doi: 10.1016/S0957-4166(00)86276-X.
Soloshonok V.A., Hayashi T. Gold(I)-catalyzed asymmetric aldol reaction of methyl isocyanoacetate with fluorinated benzaldehydes. Tetrahedron Lett. 1994. 35(17): 2713–2716.
doi: 10.1016/S0040-4039(00)77013-4.
Takeda R., Kawamura A., Kawashima A. et al. Chemical dynamic kinetic resolution and S/R interconversion of unprotected α-amino acids. Angew. Chem. Int. Ed. 2014. 53(3): 12214–12217.
doi: 10.1002/anie.201407944.
Bravo P., Farina A., Kukhar V. P. et al. Stereoselective additions of α-lithiated alkyl-p-tolylsulfoxides to N-PMP fluoroalkyl aldimines. An efficient approach to enantiomerically pure fluoro amino compounds. J. Org. Chem. 1997. 62(11): 3424–3425.
doi: 10.1021/jo970004v.
Soloshonok V.A., Hayashi T. Gold(I)-catalyzed asymmetric aldol reaction of fluorinated benzaldehydes with α-isocyanoacetamide Tetrahedron: Asymmetry. 1994. 5(6): 1091–1094.
doi: 10.1016/0957-4166(94)80059-6.
Nian Y., Wang J., Zhou S. et al. Recyclable ligands for the non-enzymatic dynamic kinetic resolution of challenging α-amino acids. Angew. Chem. Int. Ed. 2015. 54(44): 12918–12922.
doi: 10.1002/anie.201507273.
Soloshonok V.A., Avilov D.V., Kukhar V.P. Asymmetric aldol reactions of trifluoromethyl ketones with a chiral Ni(II) complex of glycine: Stereocontrolling effect of the trifluoromethyl group. Tetrahedron.1996. 52(38): 12433–12442.
doi: 10.1016/0040-4020(96)00741-7.
Turcheniuk K.V., Poliashko K.O., Kukhar V.P. et al. Efficient asymmetric synthesis of trifluoromethylated β-aminophosphonates and their incorporation into dipeptides. Chem. Commun. 2012. 48(94): 11519–11521.
doi: 10.1039/C2CC36702E.
Röschenthaler G.-V., Kukhar V.P., Kulik I.B. et al. Asymmetric synthesis of phosphonotrifluoroalanine and its derivatives using N-tert-butanesulfinyl imine derived from fluoral. Tetrahedron Lett. 2012. 53(5): 539–542.
doi: 10.1016/j.tetlet.2011.11.096.
Brittain W.D., Lloyd C.M., Cobb S.L. Synthesis of complex unnatural fluorine-containing amino acids. J. Fluorine Chem. 2020. 239: 109630.
doi: 10.1016/j.jfluchem.2020.109630.
Acena J.L., Simon-Fuentes A., Fustero S. Recent developments in the synthesis of fluorinated β-amino acids. Curr. Org. Chem. 2010. 14(9): 928–949.
doi: 10.2174/138527210791111777.
Ouchakour L., Ábrahámi R.A., Forró E. et al. Stereocontrolled synthesis of fluorine‐containing piperidine γ‐amino acid derivatives. Eur. J. Org. Chem. 2019. 2019(12): 2202–2211.
doi: 10.1002/ejoc.201801540.
Zhang X.-X., Gao Y., Hu X.-S. et al. Recent advances in catalytic enantioselective synthesis of fluorinated α‐and β‐amino acids. Adv. Synth. Catal. 2020. 362(22): 4763–4793.
doi: 10.1002/adsc.202000966.
Tolman V. Syntheses of fluorinated amino acids: from the classical to the modern concept. Amino Acids. 1996. 11(1): 15–36.
doi: 10.1007/BF00805718.
Lin D., Wang J., Liu H. Recent developments in the synthesis of fluorine-containing β-amino acids and β-lactams. Chin. J. Org. Chem. 2013. 33(10): 2098–2107.
doi: 10.6023/cjoc201303020.
Albler C., Schmid W. Synthetic routes towards fluorine‐containing amino sugars: synthesis of fluorinated analogues of tomosamine and 4‐amino‐4‐deoxyarabinose. Eur. J. Org. Chem. 2014. 2014(12): 2451–2459.
doi: 10.1002/ejoc.201301614.
Vera-Ayoso Y., Borrachero P., Cabrera-Escribano F. et al. Towards cyclic, conformationally constrained, fluorine-containing β-amino acid derivatives from D-glucose. Tetrahedron: Asymmetry. 2001. 12(14): 2031–2041.
doi: 10.1016/S0957-4166(01)00354-8.
Soloshonok V.A., Kirilenko A.G., Fokina N.A. et al. Biocatalytic resolution of β-fluoroalkyl-β-amino acids. Tetrahedron: Asymmetry. 1994. 5(6): 1119–1126.
doi: 10.1016/0957-4166(94)80063-4.
Yamada T., Okada T., Sakaguchi K. et al. Efficient asymmetric synthesis of novel 4-substituted and configurationally stable analogues of thalidomide. Org. Lett. 2006, 8(24): 5625–5628.
doi: 10.1021/ol0623668.
Shibata N., Nishimine T., Shibata N. et al. Organic base-catalyzed stereodivergent synthesis of (R)- and (S)-3-amino-4,4,4-trifluorobutanoic acids. Chem. Commun. 2012. 48(34): 4124–4126.
doi: 10.1039/C2CC30627A.
Soloshonok V.A., Kirilenko A.G., Kukhar V.P., Resnati G. Transamination of fluorinated β-keto carboxylic esters. A biomimetic approach to β-polyfluoroalkyl-β-amino acids. Tetrahedron Lett. 1993. 34(22): 3621–3624.
doi: 10.1016/S0040-4039(00)73652-5.
Soloshonok V.A., Kirilenko A.G., Fokina N.A. et al. Chemo-enzymatic approach to the synthesis of each of the four isomers of α-alkyl-β-fluoroalkyl-substituted β-amino acids. Tetrahedron: Asymmetry.1994. 5(7): 1225–1228.
doi: 10.1016/0957-4166(94)80163-0.
Soloshonok V.A., Kirilenko A.G., Galushko S.V., Kukhar V.P. Catalytic asymmetric synthesis of β-fluoroalkyl-β-amino acids via biomimetic [1,3]-proton shift reaction. TetrahedronLett. 1994. 35(28): 5063–5064.
doi: 10.1016/S0040-4039(00)73320-X.
Soloshonok V.A., Ono T. The effect of substituents on the feasibility of azomethine-azomethine isomerization: New synthetic opportunities for biomimetic transamination. Tetrahedron.1996. 52(47): 14701–14712.
doi: 10.1016/0040-4020(96)00920-9.
Soloshonok V.A., Kukhar V.P. Biomimetic transamination of α-keto perfluorocarboxylic esters. An efficient preparative synthesis of β,β,β-trifluoroalanine. Tetrahedron. 1997. 53(25): 8307–8314.
doi: 10.1016/S0040-4020(97)00517-6.
Soloshonok V.A., Ono T., Soloshonok I. V. Enantioselective biomimetic transamination of β-keto carboxylic acid derivatives. An efficient asymmetric synthesis of β-fluoroalkyl β-amino acids. J. Org. Chem. 1997. 62(22): 7538–7539.
doi: 10.1021/jo9710238.
Soloshonok V.A., Ohkura H., Yasumoto M. Operationally convenient asymmetric synthesis of (S)- and (R)-3-amino-4,4,4-trifluorobutanoic acid: Part II. Enantioselective biomimetic transamination of 4,4,4-trifluoro-3-oxo-N-[(R)-1-phenylethyl)butanamide. J. Fluorine Chem. 2006. 127(7): 930–935.
doi: 10.1016/j.jfluchem.2006.04.004.
Soloshonok V.A., Soloshonok I.V., Kukhar V.P., Svedas V.K. Biomimetic transamination of α-alkyl β-keto carboxylic esters. Chemoenzymatic approach to the stereochemically defined α-Alkyl β-Fluoroalkyl β-Amino Acids. J. Org. Chem. 1998. 63(6): 1878–1884.
doi: 10.1021/jo971777m.
Sorochinsky A., Voloshin N., Markovsky A. et al. Convenient asymmetric synthesis of β-substituted α,α-difluoro-β-amino acids via Reformatsky reaction between Davis’N-sulfinylimines and ethyl bromodifluoroacetate. J. Org. Chem. 2003. 68(19): 7448–7454.
doi: 10.1021/jo030082k.
Soloshonok V.A., Ohkura H., Sorochinsky A. et al. Convenient, large-scale asymmetric synthesis of β-aryl-substituted α,α-difluoro-β-amino acids. Tetrahedron Lett. 2002. 43(31): 5445–5448. doi: 10.1016/S0040-4039(02)01103-6.
Kukhar VP. Fluorine-containing amino acids. J. Fluorine Chem. 1994. 69(3): 199–205.
doi: 10.1016/0022-1139(94)03131-2.
Qiu X.-L., Qing F.-L. Recent advances in the synthesis of fluorinated amino acids. Eur. J. Org. Chem. 2011. 2011(18): 3261–3278.
doi: 10.1002/ejoc.201100032.
Qiu X.-L, Meng W.-D, Qing F.-L. Synthesis of fluorinated amino acids. Tetrahedron. 2004. 60(32): 6711–6745.
doi: 10.1016/j.tet.2004.05.051.
Sutherland A., Willis C.L. Synthesis of fluorinated amino acids. Nat. Prod. Rep. 2000. 17(6): 621–631.
doi: 10.1039/A707503K.
Kiss L., Fülöp F. Selective synthesis of fluorine‐containing cyclic β‐amino acid scaffolds. Chem. Rec. 2018. 18(3): 266–281.
doi: 10.1002/tcr.201700038.
Zhou M., Feng Z., Zhang X. Recent advances in the synthesis of fluorinated amino acids and peptides. Chem. Commun. 2023. 59(11): 1434–1448.
doi: 10.1039/D2CC06787K.
Moschner J., Stulberg V., Fernandes R.et al. Approaches to obtaining fluorinated α-amino acids. Chem. Rev. 2019. 119(18): 10718–10801.
doi: 10.1021/acs.chemrev.9b00024.
Mykhailiuk P.K. Fluorine-containing prolines: Synthetic strategies, applications, and opportunities. J. Org. Chem. 2022. 87(11): 6961–7005.
doi: 10.1021/acs.joc.1c02956.
Otaka A., Mitsuyama E., Watanabe J. et al. Synthesis of fluorine‐containing bioisosteres corresponding to phosphoamino acids and dipeptide units. Pept. Sci. 2004. 76(2): 140–149.
doi:10.1002/bip.10570.
Tarui A., Sato K., Omote M. et al. Stereoselective synthesis of α‐fluorinated amino acid derivatives. Adv. Synth. Catal. 2010. 352(16): 2733–2744.
doi: 10.1002/adsc.201000506.
Wang Y., Song X., Wang J. et al. Recent approaches for asymmetric synthesis of α-amino acids via homologation of Ni(II) complexes. Amino Acids. 2017. 49(9): 1487–1520.
doi: 10.1007/s00726-017-2458-6.
Soloshonok V.A. Highly diastereoselective Michael addition reactions between nucleophilic glycine equivalents and β-substituted-α,β-unsaturated carboxylic acid derivatives; a general approach to the stereochemically defined and sterically χ-constrained α-amino acids. Curr. Org. Chem. 2002. 6(4): 341–364.
doi: 10.2174/1385272024605014.
Han J., Sorochinsky A.E., Ono T., Soloshonok V.A. Biomimetic transamination - a metal-free alternative to the reductive amination. Application for generalized preparation of fluorine containing amines and amino acids. Curr. Org. Synth. 2011. 8(2): 281–294.
doi: 10.2174/157017911794697277.
Soloshonok V.A., Sorochinsky A.E. Practical methods for the synthesis of symmetrically α,α-disubstituted α-amino acids. Synthesis. 2010. 2010(14): 2319–2344.
doi: 10.1055/s-0029-1220013.
Mikami K., Fustero S., Sánchez-Roselló M. et al. Synthesis of fluorinated β-amino acids. Synthesis. 2011. 2011(19): 3045–3079.
doi: 10.1055/s-0030-1260173.
Sorochinsky A.E., Soloshonok V.A. Asymmetric synthesis of fluorine-containing amines, amino alcohols, α- and β-amino acids mediated by chiral sulfinyl group. J. Fluorine Chem. 2010. 131(2): 127–139.
doi: 10.1016/j.jfluchem.2009.09.015.
Sorochinsky A.E., Aceña J.L., H. Moriwaki H. et al. Asymmetric synthesis of α-amino acids via homologation of Ni(II) complexes of glycine Schiff bases; Part 1: alkyl halide alkylations. Amino Acids. 2013. 45(4): 691–718.
doi: 10.1007/s00726-013-1539-4.
Aceña J.L., Sorochinsky A.E., Soloshonok V.A. Recent advances in asymmetric synthesis of α-(trifluoromethyl)-containing α-amino acids. Synthesis. 2012. 44(11): 1591–1602.
doi: 10.1055/s-0031-1289756.
Sorochinsky A.E., Aceña J.L., Moriwaki H. et al. Asymmetric synthesis of α-amino acids via homologation of Ni(II) complexes of glycine Schiff bases. Part 2: Aldol, Mannich addition reactions, deracemization and (S) to (R) interconversion of α-amino acids. Amino Acids. 2013. 45(5): 1017–1033.
doi:10.1007/s00726-013-1580-3.
Aceña J.L., Sorochinsky A.E., Moriwaki H. et al. Synthesis of fluorine-containing α-amino acids in enantiomerically pure form via homologation of Ni(II) complexes of glycine and alanine Schiff bases. J. Fluorine Chem. 2013. 155: 21–38.
doi:10.1016/j.jfluchem.2013.06.004.
Aceña J.L., Sorochinsky A.E., Soloshonok V. Asymmetric synthesis of α-amino acids via homologation of Ni(II) complexes of glycine Schiff bases. Part 3: Michael addition reactions and miscellaneous transformations. Amino Acids. 2014. 46(9): 2047–2073.
doi: 10.1007/s00726-014-1764-5.
Kukhar V.P., Sorochinsky A.E., Soloshonok V.A. Practical synthesis of fluorine-containing α- and β-amino acids: recipes from Kiev, Ukraine. Future Med. Chem. 2009. 1(5): 793–819.
doi: 10.4155/fmc.09.70.
Drug Trials Snapshots: VOYDEYA. Available at https://www.fda.gov/drugs/drug-approvals- and-databases/drug-trials-snapshots-voydeya (accessed, December, 2024).
Hao J., Milcent T., Retailleau P. et al. Asymmetric synthesis of cyclic fluorinated amino acids. Eur. J. Org. Chem. 2018. 2018(27–28): 3688–3692.
doi: 10.1002/ejoc.201800255.
Sato T., Izaw K., Aceña J.L. et al. Tailor-made α-amino acids in pharmaceutical industry: synthetic approaches to (1R,2S)-1-amino-2-vinylcyclopropane-1-carboxylic acid (vinyl-ACCA). Eur. J. Org. Chem. 2016. 2016(16): 2757–2774.
doi: 10.1002/ejoc.201600112.
Yamada T., Okada T., Sakaguchi K. et al. Efficient asymmetric synthesis of novel 4-substituted and configurationally stable analogues of thalidomide. Org. Lett. 2006. 8(24): 5625–5628.
doi:10.1021/ol0623668.
Cai C., Soloshonok V.A., Hruby V.J. Michael addition reactions between chiral Ni(II) complex of glycine and 3-(trans-Enoyl)oxazolidin-2-ones. A case of electron donor−acceptor attractive interaction-controlled face diastereoselectivity. J. Org. Chem. 2001. 66(4): 1339–1350.
doi: 10.1021/jo0014865.
Soloshonok V.A., Ueki H., Tiwari R. et al. Virtually complete control of simple and face diastereoselectivity in the Michael addition reactions between achiral equivalents of a nucleophilic glycine and (S)- or (R)-3-(E-enoyl)-4-phenyl-1,3-oxazolidin-2-ones: practical method for preparation of β-substituted pyroglutamic acids and prolines.J. Org. Chem. 2004. 69(15): 4984–4990.
doi: 10.1021/jo0495438.
Soloshonok V.A., Ueki H., Ellis T.K. et al. Application of modular nucleophilic glycine equivalents for truly practical asymmetric synthesis of β-substituted pyroglutamic acids. Tetrahedron Lett. 2005. 46(7): 1107–1110.
doi: 10.1016/j.tetlet.2004.12.093.
Wiles J.A., Phadke A.S., Deshpande M., Agarwal A., Chen D., Gadhachanda V.R., Hashimoto A., Pais G., Wang Q., Wang X. Achillion Pharmaceuticals Inc. 2018. Aryl, heteroaryl, and heterocyclic compounds for treatment of medical disorders. U.S. Patent Application 2018305375 A1.
Wiles J.A., Phadke A.S., Deshpande M., Agarwal A., Chen D., Gadhachanda V. R., Hashimoto A., Pais G., Wang Q., Wang X. Achillion Pharmaceuticals Inc. 2020. Aryl, heteroaryl, and heterocyclic compounds for treatment of medical disorders. U.S. Patent 10822352 B2.
Kang C. Danicopan: first approval. Drugs. 2024. 84(5): 613–618.
doi:10.1007/s40265-024-02023-6.
Verdin P. FDA new drug approvals in Q1 2024. Nat. Rev. Drug. Discov. 2024. 23(5): 331.
doi:10.1038/d41573-024-00063-x.
Kulasekararaj A.G., Lazana I. Paroxysmal nocturnal hemoglobinuria: Where are we going. Am. J. Hematol. 2023. 98(S5): 33–43.
doi:10.1002/ajh.26882.
Voydeya (danicopan) granted first-ever regulatory approval in Japan for adults with PNH to be used in combination with C5 inhibitor therapy. Available at https://www.astrazeneca.com./media-centre/press-releases/2024/voydeya-danicopan-granted-first-ever-regulatory-approval-in-japan-for-adults-with-pnh-to-be-used-in-combination-with-c5-inhibitor-therapy.html(accessed, December, 2024).
First oral treatment against residual haemolyticanaemia in patients with paroxysmal nocturnal haemoglobinuria. Available at https://www.ema.europa.eu/en/news/first-oral-treatment-against-residual-haemolytic-anaemia-patients-paroxysmal-nocturnal-haemoglobinuria(accessed, December, 2024).
Wiles J. A., Phadke A.S., Deshpande M., Agarwak A., Chen D., Gadhachanda V.R., Hashimoto A., Pais G., Wang Q., Wang X. Achillion Pharmaceuticals Inc. 2017. Aryl, heteroaryl, and heterocyclic compounds for treatment of medical disorders. WO2017035353A1.
Phadke A., Hashimoto A., Andres M. Achillion Pharmaceuticals Inc. 2020. Morphic forms of complement factor D inhibitors. WO2020069024A1.
Phadke A. Achillion Pharmaceuticals Inc. 2020. Morphic forms of complement factor D inhibitors. WO2020051538A1.
Moore J.L., Taylor S.M., Soloshonok V.A. An efficient and operationally convenient general synthesis of tertiary amines by direct alkylation of secondary amines with alkyl halides in the presence of Huenig’sbase. Arkivoc. 2005. 2005(6): 287–292.
doi: 10.3998/ark.5550190.0006.624.
Drug Trials Snapshots: OJEMDA. Available athttps://www.fda.gov/drugs/drug-approvals-and-databases/drug-trials-snapshots-ojemda(accessed, December, 2024).
Verdin P. FDA new drug approvals in Q2 2024. Nat. Rev. Drug Discov. 2024. 23(8): 573. doi:10.1038/d41573-024-00118-z.
Dhillon S. Tovorafenib: First Approval. Drugs. 2024. 84(8). 985–993.
doi:10.1007/s40265-024-02069-6.
Chen W., Cossrow J., Franklin L. et al. Biogen Idec Inc.; Sunesis Pharmaceuticals Inc. 2010. Compounds useful as RAF kinase inhibitors. Chinese Patent CN101784545A.
Chen W., Cossrow J., Franklin L. et al. Biogen Idec Inc.; Sunesis Pharmaceuticals Inc. 2010. Compounds useful as RAF kinase inhibitors. Chinese Patent CN101784545B.
Zhang T., Xu B., Tang F., He Z., Zhou J. Type II RAF inhibitor tovorafenib for the treatment of pediatric low-grade glioma. Expert Rev. Clin. Pharmacol. 2024. 17(11): 999–1008.
doi:10.1080/17512433.2024.2418405.
Sun Y., Alberta J.A., Pilarz C. et al. A brain-penetrant RAF dimer antagonist for the noncanonical BRAF oncoprotein of pediatric low-grade astrocytomas. Neuro Oncol. 2017. 19(6): 774–785.
doi:10.1093/neuonc/now261.
FDA grants accelerated approval to tovorafenib for patients with relapsed or refractory BRAF-altered pediatric low-grade glioma. Available athttps://www.fda.gov/drugs/resources-information-approved-drugs/fda-grants-accelerated-approval-tovorafenib-patients-relapsed-or-refractory-braf-altered-pediatric(accessed, December, 2024).
Drugs@FDA: FDA-Approved Drugs. Available at https://www.accessdata.fda.gov/scripts /cder/daf/index.cfm?event=overview.process&ApplNo=218033 (accessed, December, 2024).
Hirano S., Takeda Y., Nakamoto K., Ikeuchi M., Kitayama M., Yamada M., Kawakami J. Day One Biopharmaceuticals Inc. 2020. Method for producing optically active compound. U.S. Patent Application 2020/0317659 A1.
Han J., Takeda R., Sato T. Optical Resolution of Rimantadine. Molecules. 2019. 24(9): 1828.
doi:10.3390/molecules24091828.
Turner N.C., Im S.-A., Saura C. et al. Inavolisib-based therapy in PIK3CA-mutated advanced breast cancer. N. Engl. J. Med. 2024. 391(17):1584–1596.
doi: 10.1056/NEJMoa2404625.
Bartsch R. Next generation of drugs in breast cancer. Memo - Mag. Eur. Med. Oncol. 2024. 17(4): 280–286.
doi: 10.1007/s12254-024-00999-1.
Singh S., Bradford D., Li X. et al. FDA approval summary: Alpelisib for PIK3CA-related overgrowth spectrum. Clin. Cancer Res. 2024. 30(1):23–28.
doi: 10.1158/1078-0432.CCR-23-1270.
Sirico M., D’Angelo A., Gianni C. et al. Current State and Future Challenges for PI3K Inhibitors in Cancer Therapy. Cancers. 2023. 15(3): 703.
doi: 10.3390/cancers15030703.
Salphati L., Pang J., Plise E.G. et al. Preclinical assessment of the PI3Kα selective inhibitor inavolisib and prediction of its pharmacokinetics and efficacious dose in human. Xenobiotica. 2024. 54(10): 808–820.
doi: 10.1080/00498254.2024.2415103.
Shan K.S., Bonano-Rios A., Theik N.W.Y. et al. Molecular targeting of the phosphoinositide-3-protein kinase (PI3K) pathway across various cancers. Int. J. Mol. Sci. 2024. 25(4): 1973.
doi: 10.3390/ijms25041973.
Belli C., Repetto M., Anand S. et al. The emerging role of PI3K inhibitors for solid tumour treatment and beyond. Br. J. Cancer. 2023. 128(12): 2150–2162.
doi: 10.1038/s41416-023-02221-1.
Yu M., Chen J., Xu Z. et al. Development and safety of PI3K inhibitors in cancer. Arch. Toxicol. 2023. 97(3): 635–650.
doi: 10.1007/s00204-023-03440-4.
Vanhaesebroeck B., Perry M.W.D., Brown J.R. et al. PI3K inhibitors are finally coming of age. Nat. Rev. Drug Discov. 2021. 20(10): 741–769.
doi: 10.1038/s41573-021-00209-1.
Song K.W., Edgar K.A., Hanan E.J. et al. RTK-dependent inducible degradation of mutant PI3Kα drives GDC-0077 (Inavolisib) efficacy. Cancer Discov. 2022. 12(1): 204–219.
doi: 10.1158/2159-8290.CD-21-0072.
Hanan E.J., Braun M.-G., Heald R.A. et al. Discovery of GDC-0077 (Inavolisib), a highly selective inhibitor and degrader of mutant PI3Kα. J. Med. Chem. 2022. 65(24): 16589–16621.
doi: 10.1021/acs.jmedchem.2c01422.
Ndubaku C.O., Heffron T.P., Staben S.T. et al. Discovery of 2-{3-[2-(1-isopropyl-3-methyl-1H-1,2–4-triazol-5-yl)-5,6-dihydrobenzo[f]imidazo[1,2-d][1,4]oxazepin-9-yl]-1H-pyrazol-1-yl}-2-methylpropanamide (GDC-0032): A β-sparing phosphoinositide 3-kinase inhibitor with high unbound exposure and robust in vivo antitumor activity. J. Med. Chem. 2013. 56(11): 4597–4610.
doi:10.1021/jm4003632.
Deeks E.D. Asciminib: First Approval. Drugs. 2022. 82(2): 219–226.
doi: 10.1007/s40265-021-01662-3.
Schoepfer J., Jahnke W., G. Berellini G. et al. Discovery of Asciminib (ABL001), an allosteric inhibitor of the tyrosine kinase activity of BCR-ABL1. J. Med. Chem. 2018. 61(18): 8120−8135.
doi: 10.1021/acs.jmedchem.8b01 040.
Mulik B.M., Srivastava N., Pendharkar D., Guin M. Design, aynthesis, and anticancer activity of novel methoxycyclohexylnicotinamides. Russ. J. Org. Chem. 2024. 60(1): 173–184.
doi: 10.1134/S1070428024010226.
Kurzrock R., Gutterman J.U., Talpaz M. The molecular genetics of Philadelphia chromosome-positive leukemias. N. Engl. J. Med. 1988. 319(15): 990–998.
doi: 10.1056/NEJM198810133191506.
Schuld P., Grzesiek S., Schlotte J. et al. Structural and biochemical studies confirming the mechanism of action of Asciminib, an agent specifically targeting the ABL myristoyl pocket (STAMP). Blood. 2020. 136 (Supplement 1): 34−35.
doi: 10.1182/blood-2020-140968.
Wylie A.A., Schoepfer J., Jahnke W. et al. The allosteric inhibitor ABL001 enables dual targeting of BCR-ABL1. Nature. 2017. 543(7647): 733−737.
doi: 10.1038/nature21702.
Milojkovic D., Apperley J. Mechanisms of resistance to Imatinib and second-generation Tyrosine inhibitors in chronic myeloid leukemia. Clin. Cancer Res. 2009. 15(24): 7519–7527.
doi: 10.1158/1078-0432.CCR-09-1068.
Novartis Scemblix® FDA approved in newly diagnosed CML, offering superior efficacy, and favorable safety and tolerability profile.Available athttps://www.novartis.com/news/media-releases/novartis-scemblix-fda-approved-newly-diagnosed-cml-offering-superior-efficacy-and-favorable-safety-and-tolerability-profile(accessed, December, 2024).
Blank J., Koecher C., Pachinger W.H. et al. Novartis AG. 2020. Process for the preparation of N-[4-(chlorodifluoromethoxy)phenyl]-6-[(3R)-3-hydroxypyrrolidin-1-yl]-5-(1H-pyrazol-5-yl)pyridine-3-carboxami de. WO 2020230100 A1.
Dodd S.K., Furet P., Grotzfeld R.M. et al. Novartis AG. 2013. Benzamide derivatives for inhibiting the activity of abl1, abl2 and bcr-abl1.WO 2013171639 A1.
Issa G.C., Aldoss I., Di Persio J. et al. The menin inhibitor revumenib in KMT2A-rearranged orNPM1-mutant leukaemia. Nature. 2023. 615(7954): 920–924.
doi: 10.1038/s41586-023-05812-3.
Issa G.C., Aldoss I., Di Persio J.F. et al. The menininhibitor SNDX-5613 (revumenib) leads to durable responses in patients (Pts) with KMT2A-rearranged or NPM1 mutant AML: Updated results of a phase (Ph) 1 study. Blood. 2022. 140 (Supplement 1): 150–152.
doi: 10.1182/blood-2022-164849.
Fareed A., Inam N., Faraz F. Breakthrough treatment choice for acute myeloid leukemia in pediatric and adult patients: Revumenib, an oral selective inhibitor of KMTA 2Ar. Rare Tumors. 2023. 15: 20363613231183785.
doi:10.1177/20363613231183785.
Candoni A., Coppola G.A. 2024. update on menininhibitors. A new class of target agents against KMT2A-rearranged and NPM1-mutated acute myeloid leukemia. Hematol. Rep. 2024. 16(2): 244–254.
doi: 10.3390/hematolrep16020024.
Zhou G., Liu K., Wei Y., Yuan H. Acerand Therapeutics (Hong Kong) Ltd. 2022. Diazaspirobicylic compounds as protein-protein interaction inhibitors and applications thereof. WO2022257047 A1.
Fleischmann M., Bechwar J., Voigtländer D. et al. Synergistic effects of the RAR alpha agonist Tamibarotene and the menininhibitor Revumenib in acute myeloid leukemia cells with KMT2A rearrangement or NPM1 mutation.Cancers. 2024. 16(7):1311.
doi: 10.3390/cancers16071311.
Thomas X. Small molecule menininhibitors: Novel therapeutic agents targeting acute myeloid leukemia with KMT2A rearrangement orNPM1 mutation. Oncol. Ther. 2024. 12(1): 57–72.
doi: 10.1007/s40487-024-00262-x.
Cacatian S., Claremon D.A., Dillard L.W. et al. Vitae Pharmaceuticals Inc. 2017. Inhibitors of the menin-MLL interaction. WO2017214367 A1.
Soloshonok V.A. Remarkable amplification of self-disproportionation of enantiomers on achiral-phase chromatography columns. Angew. Chem. Int. Ed. 2006. 45(5): 766–769.
doi: 10.1002/anie.200503373.
Soloshonok V.A, Ueki H., Yasumoto M. et al. Phenomenon of optical self-purification of chiral non-racemic compounds. J. Am. Chem. Soc. 2007. 129(40): 12112–12113.
doi: 10.1021/ja065603a.
Soloshonok V.A., Klika K.D. Terminology related to the phenomenon ‘self-disproportionation of enantiomers’ (SDE). Helv. Chem Acta. 2014. 97(11): 1583–1589.
doi: 10.1002/hlca.201400122.
Ueki H., Yasumoto M., Soloshonok V.A. Rational application of self-disproportionation of enantiomers via sublimation–a novel methodological dimension for enantiomeric purifications. Tetrahedron: Asymmetry. 2010. 21(11–12): 1396–1400.
doi: 10.1016/j.tetasy.2010.04.040.
Sorochinsky A.E., Katagiri T., Ono T. et al. Optical purifications via self-disproportionation of enantiomers by achiral chromatography; Case study of a series of α-CF3-containing secondary alcohols. Chirality. 2013. 25(6): 365–368.
doi: 10.1002/chir.22180.
Sorochinsky A.E., Aceña J.L., Soloshonok V.A. Self-disproportionation of enantiomers of chiral, non-racemic fluoroorganiccompounds: Role of fluorine as enabling element. Synthesis. 2013. 45(2): 141–152.
doi: 10.1055/s-0032-1316812.
Han J., Wzorek A., Kwiatkowska M. et al. The self-disproportionation of enantiomers (SDE) of amino acids and their derivatives. Amino Acids. 2019. 5 1(6): 865–889.
doi: 10.1007/s00726-019-02729-y.
Wzorek A., Sato A., Drabowicz J. et al. Remarkable magnitude of the self-disproportionation of enantiomers (SDE) via achiral chromatography; application to the practical-scale enantiopurification of β-amino acid esters. Amino Acids. 2016. 48(2): 605–613.
doi: 10.1007/s00726-015-2152-5.
Hosaka T., Imai T., Wzorek A. et al. The self-disproportionation of enantiomers (SDE) of α-amino acid derivatives; facets of steric and electronic properties. Amino Acids. 2019. 51(2): 283–294.
doi: 10.1007/s00726-018-2664-x.
Soloshonok V.A., Wzorek A., Klika K.D. A question of policy: should tests for the self-disproportionation of enantiomers (SDE) be mandatory for reports involving scalemates? Tetrahedron: Asymmetry. 2017. 28(10): 1430–1434.
doi: 10.1016/j.tetasy.2017.08.020.
Han J., Soloshonok V.A., Klika K.D. et al.. Chiral sulfoxides: advances in asymmetric synthesis and problems with the accurate determination of the stereochemical outcome. Chem. Soc. Rev. 2018. 47(4): 1307–1350.
doi: 10.1039/c6cs00703a.
Soloshonok V.A., Roussel C., Kitagawa O., Sorochinsky A.E. Self-disproportionation of Enantiomers via achiral chromatography: a warning and extra dimension in optical purifications. Chem. Soc. Rev. 2012. 41(11): 4180–4188.
doi:10.1039/C2CS35006H.
Han J., Kitagawa O., Wzorek A. et al. The self-disproportionation of enantiomers (SDE): a menace or an opportunity? Chem. Sci. 2018. 9(7): 1718–1739.
doi: 10.1039/C7SC05138G.