Discovery of potent heat shock protein 90 (Hsp90) inhibitors: structure-based virtual screening, molecular dynamics simulation, and biological evaluation

References

• Hu C, Yang J, Qi Z, Wu H, Wang B, Zou F, Mei H, Liu J, Wang W, Liu Q, et al. Heat shock proteins: biological functions, pathological roles, and therapeutic opportunities. MedComm. 2022;3(3):e161.
   PubMedGoogle Scholar
• Calderwood SK, Khaleque MA, Sawyer DB, Ciocca DR. Heat shock proteins in cancer: chaperones of tumorigenesis. Trends Biochem Sci. 2006;31(3):164–172.
   PubMed Web of Science ®Google Scholar
• Wang L, Xu XL, Jiang ZY, You QD. Modulation of protein fate decision by small molecules: targeting molecular chaperone machinery. Acta Pharm Sin B. 2020;10(10):1904–1925.
   PubMed Web of Science ®Google Scholar
• Dhamad AE, Zhou ZQ, Zhou JH, Du YC. Systematic proteomic identification of the heat shock proteins (Hsp) that interact with estrogen receptor alpha (ERα) and biochemical characterization of the ERα-Hsp70 interaction. PLoS One. 2016;11(8):e0160312.
   PubMed Web of Science ®Google Scholar
• Bickel D, Gohlke H. C-terminal modulators of heat shock protein of 90kDa (HSP90): state of development and modes of action. Bioorg Med Chem. 2019;27(21):115080.
   PubMed Web of Science ®Google Scholar
• Kim S-H, Bajji A, Tangallapally R, Markovitz B, Trovato R, Shenderovich M, Baichwal V, Bartel P, Cimbora D, McKinnon R, et al. Discovery of (2S)-1-[4-(2-{6-amino-8-[(6-bromo-1,3-benzodioxol-5-yl)sulfanyl]-9H-purin-9-yl}ethyl)piperidin-1-yl]-2-hydroxypropan-1-one (MPC-3100), a purine-based Hsp90 inhibitor. J Med Chem. 2012;55(17):7480–7501.
   PubMed Web of Science ®Google Scholar
• Samant RS, Clarke PA, Workman P. The expanding proteome of the molecular chaperone HSP90. Cell Cycle. 2012;11(7):1301–1308.
   PubMed Web of Science ®Google Scholar
• Prince T, Neckers L. A network of its own: the unique interactome of the Hsp90 cochaperone, Sba1/p23. Mol Cell. 2011;43(2):159–160.
   PubMed Web of Science ®Google Scholar
• Echeverria PC, Bernthaler A, Dupuis P, Mayer B, Picard D. An interaction network predicted from public data as a discovery tool: application to the Hsp90 molecular chaperone machine. PLoS One. 2011;6(10):e26044.
   PubMed Web of Science ®Google Scholar
• Wagner AJ, Chugh R, Rosen LS, Morgan JA, George S, Gordon M, Dunbar J, Normant E, Grayzel D, Demetri GD, et al. A phase I study of the HSP90 inhibitor retaspimycin hydrochloride (IPI-504) in patients with gastrointestinal stromal tumors or soft-tissue sarcomas. Clin Cancer Res. 2013;19(21):6020–6029.
   PubMed Web of Science ®Google Scholar
• Mori M, Hitora T, Nakamura O, Yamagami Y, Horie R, Nishimura H, Yamamoto T. Hsp90 inhibitor induces autophagy and apoptosis in osteosarcoma cells. Int J Oncol. 2015;46(1):47–54.
   PubMed Web of Science ®Google Scholar
• Zhang T, Hamza A, Cao X, Wang B, Yu S, Zhan C-G, Sun D. A novel Hsp90 inhibitor to disrupt Hsp90/Cdc37 complex against pancreatic cancer cells. Mol Cancer Ther. 2008;7(1):162–170.
   PubMed Web of Science ®Google Scholar
• Patel HJ, Modi S, Chiosis G, Taldone T. Advances in the discovery and development of heat-shock protein 90 inhibitors for cancer treatment. Expert Opin Drug Discov. 2011;6(5):559–587.
   PubMed Web of Science ®Google Scholar
• Mak OW, Sharma N, Reynisson J, Leung IKH. Discovery of novel Hsp90 C-terminal domain inhibitors that disrupt co-chaperone binding. Bioorg Med Chem Lett. 2021;38:127857.
   PubMed Web of Science ®Google Scholar
• Verba KA, Wang RY-R, Arakawa A, Liu Y, Shirouzu M, Yokoyama S, Agard DA. Atomic structure of Hsp90-Cdc37-Cdk4 reveals that Hsp90 traps and stabilizes an unfolded kinase. Science. 2016;352(6293):1542–1547.
   PubMed Web of Science ®Google Scholar
• Matts RL, Dixit A, Peterson LB, Sun L, Voruganti S, Kalyanaraman P, Hartson SD, Verkhivker GM, Blagg BSJ. Elucidation of the Hsp90 C-terminal inhibitor binding site. ACS Chem Biol. 2011;6(8):800–807.
   PubMed Web of Science ®Google Scholar
• Kim HH, Hyun JS, Choi J, Choi KE, Jee JG, Park SJ. Structural ensemble-based docking simulation and biophysical studies discovered new inhibitors of Hsp90 N-terminal domain. Sci Rep. 2018;8(1):368.
   PubMedGoogle Scholar
• Kim S-H, Tangallapally R, Kim IC, Trovato R, Parker D, Patton JS, Reeves L, Bradford C, Wettstein D, Baichwal V, et al. Discovery of an L-alanine ester prodrug of the Hsp90 inhibitor, MPC-3100. Bioorg Med Chem Lett. 2015;25(22):5254–5257.
   PubMed Web of Science ®Google Scholar
• Sequist LV, Gettinger S, Senzer NN, Martins RG, Jänne PA, Lilenbaum R, Gray JE, Iafrate AJ, Katayama R, Hafeez N, et al. Activity of IPI-504, a novel heat-shock protein 90 inhibitor, in patients with molecularly defined non-small-cell lung cancer. J Clin Oncol. 2010;28(33):4953–4960.
   PubMed Web of Science ®Google Scholar
• Normant E, Paez G, West KA, Lim AR, Slocum KL, Tunkey C, McDougall J, Wylie AA, Robison K, Caliri K, et al. The Hsp90 inhibitor IPI-504 rapidly lowers EML4-ALK levels and induces tumor regression in ALK-driven NSCLC models. Oncogene. 2011;30(22):2581–2586.
   PubMed Web of Science ®Google Scholar
• Wang H, Lu MJ, Yao MQ, Zhu W. Effects of treatment with an Hsp90 inhibitor in tumors based on 15 phase II clinical trials. Mol Clin Oncol. 2016;5(3):326–334.
   PubMedGoogle Scholar
• Sharp SY, Boxall K, Rowlands M, Prodromou C, Roe SM, Maloney A, Powers M, Clarke PA, Box G, Sanderson S, et al. In vitro biological characterization of a novel, yynthetic diaryl pyrazole resorcinol class of heat shock protein 90 inhibitors. Cancer Res. 2007;67(5):2206–2216.
   PubMed Web of Science ®Google Scholar
• Massey AJ, Schoepfer J, Brough PA, Brueggen J, Chène P, Drysdale MJ, Pfaar U, Radimerski T, Ruetz S, Schweitzer A, et al. Preclinical antitumor activity of the orally available heat shock protein 90 inhibitor NVP-BEP800. Mol Cancer Ther. 2010;9(4):906–919.
   PubMed Web of Science ®Google Scholar
• Chen WG, Sin SH, Wen KW, Damania B, Dittmer DP. Hsp90 inhibitors are efficacious against Kaposi Sarcoma by enhancing the degradation of the essential viral gene LANA, of the viral co-receptor EphA2 as well as other client proteins. PLoS Pathog. 2012;8(11):e1003048.
   PubMed Web of Science ®Google Scholar
• Jhaveri K, Taldone T, Modi S, Chiosis G. Advances in the clinical development of heat shock protein 90 (Hsp90) inhibitors in cancers. Biochim Biophys Acta. 2012;1823(3):742–755.
   PubMed Web of Science ®Google Scholar
• Li ZN, Luo Y. HSP90 inhibitors and cancer: prospects for use in targeted therapies (Review). Oncol Rep. 2022;49(1):6.
   PubMed Web of Science ®Google Scholar
• Yang D‐S, Yang Y‐H, Zhou Y, Yu L‐L, Wang R‐H, Di B, Niu M‐M. A redox-triggered bispecific supramolecular nano-medicine based on peptide self-assembly for high-efficacy and low-toxic cancer therapy. Adv Funct Mater. 2020;30(4):1904969.
   Web of Science ®Google Scholar
• Moreira BP, Batista ICA, Tavares NC, Armstrong T, Gava SG, Torres GP, Mourão MM, Falcone FH. Docking-based virtual screening enables prioritizing protein kinase inhibitors with in vitro phenotypic activity against schistosoma mansoni. Front Cell Infect Microbiol. 2022;12:913301.
   PubMed Web of Science ®Google Scholar
• Zinovjev K, van der Kamp MW. Enlighten2: molecular dynamics simulations of protein-ligand systems made accessible. Bioinformatics. 2020;36(20):5104–5106.
   PubMed Web of Science ®Google Scholar
• Wang YT, Zhang H, Li JD, Niu M-M, Zhou Y, Qu YQ. Discovery of potent and noncovalent KRASG12D inhibitors: structure-based virtual screening and biological evaluation. Front Pharmacol. 2022;13:1094887.
   PubMed Web of Science ®Google Scholar
• Uno T, Kawai Y, Yamashita S, Oshiumi H, Yoshimura C, Mizutani T, Suzuki T, Chong KT, Shigeno K, Ohkubo M, et al. Discovery of 3-Ethyl-4-(3-isopropyl-4-(4-(1-methyl-1 H-pyrazol-4-yl)-1 H-imidazol-1-yl)-1 H-pyrazolo[3,4-b]pyridin-1-yl)benzamide (TAS-116) as a potent, selective, and orally available HSP90 inhibitor. J Med Chem. 2019;62(2):531–551.
   PubMed Web of Science ®Google Scholar
• Llauger L, He H, Kim J, Aguirre J, Rosen N, Peters U, Davies P, Chiosis G. Evaluation of 8-arylsulfanyl, 8-arylsulfoxyl, and 8-arylsulfonyl adenine derivatives as inhibitors of the heat shock protein 90. J Med Chem. 2005;48(8):2892–2905.
   PubMed Web of Science ®Google Scholar
• Molla M, Aljahdali M, Sumon M, Asseri A, Altayb H, Islam M, Alsaiari A, Opo F, Jahan N, Ahammad F, et al. Integrative ligand-based pharmacophore modeling, virtual screening, and molecular docking simulation approaches identified potential lead compounds against pancreatic cancer by targeting FAK1. Pharmaceuticals. 2023;16(1):120.
   Web of Science ®Google Scholar
• Zhou YJ, Tang S, Chen TT, Niu M-M. Structure-based pharmacophore modeling, virtual screening, molecular docking and biological evaluation for identification of Potential Poly (ADP-Ribose) Polymerase-1 (PARP-1) inhibitors. Molecules. 2019;24(23):4258.
   PubMed Web of Science ®Google Scholar
• Hu C, Guo T, Zou Y, Gao J, Gao Y, Niu M, Xia Y, Shen X, Li J. Discovery of dual S-RBD/NRP1-targeting peptides: structure-based virtual screening, synthesis, biological evaluation, and molecular dynamics simulation studies. J Enzyme Inhib Med Chem. 2023;38(1):2212327.
   PubMed Web of Science ®Google Scholar
• Kim J, Felts S, Llauger L, He H, Huezo H, Rosen N, Chiosis G. Development of a fluorescence polarization assay for the molecular chaperone Hsp90. J Biomol Screen. 2004;9(5):375–381.
   PubMedGoogle Scholar
• Zheng L, Ren R, Sun X, Zou Y, Shi Y, Di B, Niu M-M. Discovery of a dual tubulin and Poly(ADP-Ribose) polymerase-1 inhibitor by structure-based pharmacophore modeling, virtual screening, molecular docking, and biological evaluation. J Med Chem. 2021;64(21):15702–15715.
   PubMed Web of Science ®Google Scholar
• Franke J, Eichner S, Zeilinger C, Kirschning A. Targeting heat-shock-protein 90 (Hsp90) by natural products: geldanamycin, a show case in cancer therapy. Nat Prod Rep. 2013;30(10):1299–1323.
   PubMed Web of Science ®Google Scholar