Login Register Cart 0
Patent News

用于治疗冠状病毒（新冠肺炎）的新型半胱氨酸蛋白酶抑制剂的研究

卷 31, 期 9, 2024

发表于: 19 June, 2023

页: [1165 - 1169] 页: 5

弟呕挨: 10.2174/0929867330666230519163305

open access plus

摘要

本申请描述了具有弹头的化合物，例如通式化合物，以及它们在治疗医学疾病或病症（例如病毒感染）中的用途。包括具有弹头的各种化合物的药物组合物和合成方法。这些化合物是蛋白酶的抑制剂，例如3C、CL-或3CL-样蛋白酶。

关键词: 半胱氨酸蛋白酶抑制剂，新冠肺炎，半胱氨酸蛋白酶，3C样蛋白酶，奈玛特韦片/利托那韦片组合包装，莫努匹拉韦。

« Previous
[1]
Ábrányi-Balogh, P.; Petri, L.; Imre, T.; Szijj, P.; Scarpino, A.; Hrast, M. Mitrović A.; Fonovič U.P.; Németh, K.; Barreteau, H.; Roper, D.I.; Horváti, K.; Ferenczy, G.G.; Kos, J.; Ilaš, J.; Gobec, S.; Keserű G.M. A road map for prioritizing warheads for cysteine targeting covalent inhibitors. Eur. J. Med. Chem., 2018, 160, 94-107.
[http://dx.doi.org/10.1016/j.ejmech.2018.10.010] [PMID: 30321804]
[2]
Yu, W.; Zhao, Y.; Ye, H.; Wu, N.; Liao, Y.; Chen, N.; Li, Z.; Wan, N.; Hao, H.; Yan, H.; Xiao, Y.; Lai, M. Structure-based design of a dual-targeted covalent inhibitor against papain-like and main proteases of SARS-CoV-2. J. Med. Chem., 2022, 65(24), 16252-16267.
[http://dx.doi.org/10.1021/acs.jmedchem.2c00954] [PMID: 36503248]
[3]
Ullrich, S.; Nitsche, C. SARS‐CoV‐2 papain‐like protease: Structure, function and inhibition. ChemBioChem, 2022, 23(19), e202200327.
[http://dx.doi.org/10.1002/cbic.202200327] [PMID: 35993805]
[4]
Alzyoud, L.; Ghattas, M.A.; Atatreh, N. Allosteric binding sites of the SARS-CoV-2 main protease: Potential targets for broad-spectrum anti-coronavirus agents. Drug Des. Devel. Ther., 2022, 16, 2463-2478.
[http://dx.doi.org/10.2147/DDDT.S370574] [PMID: 35941927]
[5]
Cherqaoui, D.; Oubahmane, M.; Hdoufane, I.; Bjij, I.; Lahcen, N.A.; Villemin, D.; Daoud, R.; Allali, A.E. Host cell proteases mediating SARS-CoV-2 entry: An overview. Curr. Top. Med. Chem., 2022, 22(21), 1776-1792.
[http://dx.doi.org/10.2174/1568026622666220726122339] [PMID: 35894476]
[6]
Hu, Q.; Xiong, Y.; Zhu, G.H.; Zhang, Y.N.; Zhang, Y.W.; Huang, P.; Ge, G.B. The SARS-CoV-2 main protease (Mpro): Structure, function, and emerging therapies for COVID-19. MedComm, 2020, 3(3), e151.
[http://dx.doi.org/10.1002/mco2.151]
[7]
Ng, T.I.; Correia, I.; Seagal, J.; DeGoey, D.A.; Schrimpf, M.R.; Hardee, D.J.; Noey, E.L.; Kati, W.M. Antiviral drug discovery for the treatment of COVID-19 infections. Viruses, 2022, 14(5), 961.
[http://dx.doi.org/10.3390/v14050961] [PMID: 35632703]
[8]
Cannalire, R.; Cerchia, C.; Beccari, A.R.; Di Leva, F.S.; Summa, V. Targeting SARS-CoV-2 proteases and polymerase for COVID-19 treatment: State of the art and future opportunities. J. Med. Chem., 2022, 65(4), 2716-2746.
[http://dx.doi.org/10.1021/acs.jmedchem.0c01140] [PMID: 33186044]
[9]
Adedeji, A.O.; Sarafianos, S.G. Antiviral drugs specific for coronaviruses in preclinical development. Curr. Opin. Virol., 2014, 8, 45-53.
[http://dx.doi.org/10.1016/j.coviro.2014.06.002] [PMID: 24997250]
[10]
Amin, S.A.; Banerjee, S.; Ghosh, K.; Gayen, S.; Jha, T. Protease targeted COVID-19 drug discovery and its challenges: Insight into viral main protease (Mpro) and papain-like protease (PLpro) inhibitors. Bioorg. Med. Chem., 2021, 29, 115860.
[http://dx.doi.org/10.1016/j.bmc.2020.115860] [PMID: 33191083]
[11]
Dragovich, P.S.; Webber, S.E.; Babine, R.E.; Fuhrman, S.A.; Patick, A.K.; Matthews, D.A.; Lee, C.A.; Reich, S.H.; Prins, T.J.; Marakovits, J.T.; Littlefield, E.S.; Zhou, R.; Tikhe, J.; Ford, C.E.; Wallace, M.B.; Meador, J.W., III; Ferre, R.A.; Brown, E.L.; Binford, S.L.; Harr, J.E.V.; DeLisle, D.M.; Worland, S.T. Structure-based design, synthesis, and biological evaluation of irreversible human rhinovirus 3C protease inhibitors. 1. Michael acceptor structure-activity studies. J. Med. Chem., 1998, 41(15), 2806-2818.
[http://dx.doi.org/10.1021/jm980068d] [PMID: 9667970]
[12]
Vandyck, K.; Abdelnabi, R.; Gupta, K.; Jochmans, D.; Jekle, A.; Deval, J.; Misner, D.; Bardiot, D.; Foo, C.S.; Liu, C.; Ren, S.; Beigelman, L.; Blatt, L.M.; Boland, S.; Vangeel, L.; Dejonghe, S.; Chaltin, P.; Marchand, A.; Serebryany, V.; Stoycheva, A.; Chanda, S.; Symons, J.A.; Raboisson, P.; Neyts, J. ALG-097111, a potent and selective SARS-CoV-2 3-chymotrypsin-like cysteine protease inhibitor exhibits in vivo efficacy in a Syrian hamster model. Biochem. Biophys. Res. Commun., 2021, 555, 134-139.
[http://dx.doi.org/10.1016/j.bbrc.2021.03.096] [PMID: 33813272]

Rights & Permissions Print Cite
Article Metrics
41
3
© 2024 Bentham Science Publishers | Privacy Policy