795
Views
8
CrossRef citations to date
0
Altmetric
Original Article

Some sulfonamide drugs inhibit ATPase activity of heat shock protein 90: investigation by docking simulation and experimental validation

, &
Pages 603-609 | Received 26 Apr 2010, Accepted 15 Nov 2010, Published online: 29 Dec 2010

References

  • Mahalingam D, Swords R, Carew JS, Nawrocki ST, Bhalla K, Giles FJ. Targeting HSP90 for cancer therapy. Br J Cancer 2009, 100, 1523–1529.
  • Chiosis G, Rodina A, Moulick K. Emerging Hsp90 inhibitors: from discovery to clinic. Anticancer Agents Med Chem 2006, 6, 1–8.
  • Dymock BW, Drysdale MJ, McDonald E, Workman P. Inhibitors of Hsp90 and other chaperones for the treatment of cancer. Expert Opin Ther Pat 2004, 14, 837–847.
  • Isaacs JS, Xu W, Neckers L. Heat shock protein 90 as a molecular target for cancer therapeutics. Cancer Cell 2003, 3, 213–217.
  • Workman P. Altered states: selectively drugging the Hsp90 cancer chaperone. Trends Mol Med 2004, 10, 47–51.
  • Chiosis G, Vilenchik M, Kim J, Solit D. Hsp90: the vulnerable chaperone. Drug Discov Today 2004, 9, 881–888.
  • Whitesell L, Lindquist SL. HSP90 and the chaperoning of cancer. Nat Rev Cancer 2005, 5, 761–772.
  • Janin YL. Heat shock protein 90 inhibitors. A text book example of medicinal chemistry? J Med Chem 2005, 48, 7503–7512.
  • Chiosis G. Targeting chaperones in transformed systems–a focus on Hsp90 and cancer. Expert Opin Ther Targets 2006, 10, 37–50.
  • Kamal A, Boehm MF, Burrows FJ. Therapeutic and diagnostic implications of Hsp90 activation. Trends Mol Med 2004, 10, 283–290.
  • Neckers L, Neckers K. Heat-shock protein 90 inhibitors as novel cancer chemotherapeutics—an update. Expert Opin Emerg Drugs 2005, 10, 137–149.
  • Drysdale MJ, Brough PA, Massey A, Jensen MR, Schoepfer J. Targeting Hsp90 for the treatment of cancer. Curr Opin Drug Discov Devel 2006, 9, 483–495.
  • Powers MV, Workman P. Targeting of multiple signalling pathways by heat shock protein 90 molecular chaperone inhibitors. Endocr Relat Cancer 2006, 13(Suppl. 1), S125–S135.
  • Xu W, Neckers L. Targeting the molecular chaperone heat shock protein 90 provides a multifaceted effect on diverse cell signaling pathways of cancer cells. Clin Cancer Res 2007, 13, 1625–1629.
  • Workman P, Burrows F, Neckers L, Rosen N. Drugging the cancer chaperone HSP90: combinatorial therapeutic exploitation of oncogene addiction and tumor stress. Ann N Y Acad Sci 2007, 1113, 202–216.
  • Pearl LH, Prodromou C, Workman P. The Hsp90 molecular chaperone: an open and shut case for treatment. Biochem J 2008, 410, 439–453.
  • Maloney A, Workman P. Phase I pharmacokinetic and pharmacodynamic study of 17-allylamino, 17-demethoxygeldanamycin in patients with advanced malignancies. Expert Opin Biol Ther 2002, 2, 3–24.
  • Schulte TW, Neckers LM. The benzoquinone ansamycin 17-allylamino-17-demethoxygeldanamycin binds to HSP90 and shares important biologic activities with geldanamycin. Cancer Chemother Pharmacol 1998, 42, 273–279.
  • Banerji U, O’Donnell A, Scurr M, Pacey S, Stapleton S, Asad Y, Simmons L, Maloney A, Raynaud F, Campbell M, Walton M, Lakhani S, Kaye S, Workman P, Judson I. Phase I pharmacokinetic and pharmacodynamic study of 17-allylamino, 17-demethoxygeldanamycin in patients with advanced malignancies. J Clin Oncol 2005, 23, 4152–4161.
  • Goetz MP, Toft D, Reid J, Ames M, Stensgard B, Safgren S, Adjei AA, Sloan J, Atherton P, Vasile V, Salazaar S, Adjei A, Croghan G, Erlichman C. Phase I trial of 17-allylamino-17-demethoxygeldanamycin in patients with advanced cancer. J Clin Oncol 2005, 23, 1078–1087.
  • Weigel BJ, Blaney SM, Reid JM, Safgren SL, Bagatell R, Kersey J, Neglia JP, Ivy SP, Ingle AM, Whitesell L, Gilbertson RJ, Krailo M, Ames M, Adamson PC. A phase I study of 17-allylaminogeldanamycin in relapsed/refractory pediatric patients with solid tumors: a Children’s Oncology Group study. Clin Cancer Res 2007, 13, 1789–1793.
  • Modi S, Stopeck AT, Gordon MS, Mendelson D, Solit DB, Bagatell R, Ma W, Wheler J, Rosen N, Norton L, Cropp GF, Johnson RG, Hannah AL, Hudis CA. Combination of trastuzumab and tanespimycin (17-AAG, KOS-953) is safe and active in trastuzumab-refractory HER-2 overexpressing breast cancer: a phase I dose-escalation study. J Clin Oncol 2007, 25, 5410–5417.
  • Egorin MJ, Rosen DM, Wolff JH, Callery PS, Musser SM, Eiseman JL. Metabolism of 17-(allylamino)-17-demethoxygeldanamycin (NSC 330507) by murine and human hepatic preparations. Cancer Res 1998, 58, 2385–2396.
  • Kelland LR, Sharp SY, Rogers PM, Myers TG, Workman P. DT-Diaphorase expression and tumor cell sensitivity to 17-allylamino, 17-demethoxygeldanamycin, an inhibitor of heat shock protein 90. J Natl Cancer Inst 1999, 91, 1940–1949.
  • Kaur G, Belotti D, Burger AM, Fisher-Nielson K, Borsotti P, Riccardi E, Thillainathan J, Hollingshead M, Sausville EA, Giavazzi R. Antiangiogenic properties of 17-(dimethylaminoethylamino)-17-demethoxygeldanamycin: an orally bioavailable heat shock protein 90 modulator. Clin Cancer Res 2004, 10, 4813–4821.
  • Ge J, Normant E, Porter JR, Ali JA, Dembski MS, Gao Y, Georges AT, Grenier L, Pak RH, Patterson J, Sydor JR, Tibbitts TT, Tong JK, Adams J, Palombella VJ. Design, synthesis, and biological evaluation of hydroquinone derivatives of 17-amino-17-demethoxygeldanamycin as potent, water-soluble inhibitors of Hsp90. J Med Chem 2006, 49, 4606–4615.
  • Sydor JR, Normant E, Pien CS, Porter JR, Ge J, Grenier L, Pak RH, Ali JA, Dembski MS, Hudak J, Patterson J, Penders C, Pink M, Read MA, Sang J, Woodward C, Zhang Y, Grayzel DS, Wright J, Barrett JA, Palombella VJ, Adams J, Tong JK. Development of 17-allylamino-17-demethoxygeldanamycin hydroquinone hydrochloride (IPI-504), an anti-cancer agent directed against Hsp90. Proc Natl Acad Sci USA 2006, 103, 17408–17413.
  • Chiosis G, Caldas Lopes E, Solit D. Heat shock protein-90 inhibitors: a chronicle from geldanamycin to today’s agents. Curr Opin Investig Drugs 2006, 7, 534–541.
  • DeBoer C, Meulman PA, Wnuk RJ, Peterson DH. Geldanamycin, a new antibiotic. J Antibiot 1970, 23, 442–447.
  • Supko JG, Hickman RL, Grever MR, Malspeis L. Preclinical pharmacologic evaluation of geldanamycin as an antitumor agent. Cancer Chemother Pharmacol 1995, 36, 305–315.
  • Neckers L, Schulte TW, Mimnaugh E. Geldanamycin as a potential anti-cancer agent: its molecular target and biochemical activity. Invest New Drugs 1999, 17, 361–373.
  • Soga S, Shiotsu Y, Akinaga S, Sharma SV. Development of radicicol analogues. Curr Cancer Drug Targets 2003, 3, 359–369.
  • Chiosis G, Kang Y, Sun W. Discovery and development of purine-scaffold Hsp90 inhibitors. Expert Opinion on Drug Discov 2008, 3, 99–114.
  • McDonald E, Jones K, Brough PA, Drysdale MJ, Workman P. Discovery and development of pyrazole-scaffold Hsp90 inhibitors. Curr Top Med Chem 2006, 6, 1193–1203.
  • Taldone T, Gozman A, Maharaj R, Chiosis G. Targeting Hsp90: small-molecule inhibitors and their clinical development. Curr Opin Pharmacol 2008, 8, 370–374.
  • Messaoudi S, Peyrat JF, Brion JD, Alami M. Recent advances in Hsp90 inhibitors as antitumor agents. Anticancer Agents Med Chem 2008, 8, 761–782.
  • Biamonte MA, Van de Water R, Arndt JW, Scannevin RH, Perret D, Lee WC. Heat shock protein 90: inhibitors in clinical trials. J Med Chem 2010, 53, 3–17.
  • Ganesh T, Thepchatri P, Li L, Du Y, Fu H, Snyder JP, Sun A. Synthesis and SAR study of N-(4-hydroxy-3-(2-hydroxynaphthalene-1-yl)phenyl)-arylsulfonamides: heat shock protein 90 (Hsp90) inhibitors with submicromolar activity in an in vitro assay. Bioorg Med Chem Lett 2008, 18, 4982–4987.
  • Barril X, Brough P, Drysdale M, Hubbard RE, Massey A, Surgenor A, Wright L. Structure-based discovery of a new class of Hsp90 inhibitors. Bioorg Med Chem Lett 2005, 15, 5187–5191.
  • Abel G, Connors TA, Goddard P, Hoellinger H, Nguyen-Hoang-Nam, Pichat L, Ross WC, Wilman DE. Cytotoxic sulphonamides designed for selective deposition in malignant tissue. Eur J Cancer 1975, 11, 787–793.
  • Casini A, Scozzafava A, Mastrolorenzo A, Supuran LT. Sulfonamides and sulfonylated derivatives as anticancer agents. Curr Cancer Drug Targets 2002, 2, 55–75.
  • Avila C, Hadden MK, Ma Z, Kornilayev BA, Ye QZ, Blagg BS. High-throughput screening for Hsp90 ATPase inhibitors. Bioorg Med Chem Lett 2006, 16, 3005–3008.
  • Lanzetta PA, Alvarez LJ, Reinach PS, Candia OA. An improved assay for nanomole amounts of inorganic phosphate. Anal Biochem 1979, 100, 95–97.
  • Christopher A, Boris A K, Brian S J. Development and optimization of a useful assay for determining Hsp90s inherent ATPase activity. Bioorg Med Chem 2006, 14, 1134–1142.
  • Venkatachalam CM, Jiang X, Oldfield T, Waldman M. LigandFit: a novel method for the shape-directed rapid docking of ligands to protein active sites. J Mol Graph Model 2003, 21, 289–307.
  • Böhm HJ. The development of a simple empirical scoring function to estimate the binding constant for a protein–ligand complex of known three-dimensional structure. J Comput Aided Mol Des 1994, 8, 243–256.
  • Muegge I. A knowledge-based scoring function for protein–ligand interactions: probing the reference state. Perspect Drug Discovery Des 2000, 20, 99–114.
  • Muegge I, Martin YC. A general and fast scoring function for protein–ligand interactions: a simplified potential approach. J Med Chem 1999, 42, 791–804.
  • Muegge I. Effect of ligand volume correction on PMF scoring. J Comput Chem 2001, 22, 418–425.
  • Böhm HJ. Prediction of binding constants of protein ligands: a fast method for the prioritization of hits obtained from de novo design or 3D database search programs. J Comput Aided Mol Des 1998, 12, 309–323.
  • Jain AN. Scoring noncovalent protein–ligand interactions: a continuous differentiable function tuned to compute binding affinities. J Comput Aided Mol Des 1996, 10, 427–440.
  • Rowlands YM, Newbatt CP, Laurence HP, Paul W, Wynne A. High-throughput screening assay for inhibitors of heat-shock protein 90 ATPase activity. Analyt Biochem 2004, 327, 176–183.
  • Matts RL, Manjarrez JR. Assays for identification of Hsp90 inhibitors and biochemical methods for discriminating their mechanism of action. Curr Top Med Chem 2009, 9, 1462–1478.
  • Schulz-Gasch T, Stahl M. Scoring functions for protein–ligand interactions: a critical perspective. Drug Discov Today 2004, 1, 231–239.
  • Tame JR. Scoring functions: a view from the bench. J Comput Aided Mol Des 1999, 13, 99–108.
  • Krovat EM, Langer T. Impact of scoring functions on enrichment in docking-based virtual screening: an application study on renin inhibitors. J Chem Inf Comput Sci 2004, 44, 1123–1129.
  • Clark RD, Strizhev A, Leonard JM, Blake JF, Matthew JB. Consensus scoring for ligand/protein interactions. J Mol Graph Model 2002, 20, 281–295.
  • Miklos F. Consensus scoring for protein–ligand interactions. Drug Discov Today, 2006, 11, 421–428.
  • Song CM, Lim SJ, Tong JC. Recent advances in computer-aided drug design. Brief Bioinformatics 2009, 10, 579–591.
  • Jorgensen WL. Efficient drug lead discovery and optimization. Acc Chem Res 2009, 42, 724–733.
  • Leach AR, Shoichet BK, Peishoff CE. Prediction of protein–ligand interactions. Docking and scoring: successes and gaps. J Med Chem 2006, 49, 5851–5855.
  • Krovat EM, Langer T. Impact of scoring functions on enrichment in docking-based virtual screening: an application study on renin inhibitors. J Chem Inf Comput Sci 2004, 44, 1123–1129.
  • Klebe G. Virtual ligand screening: strategies, perspectives and limitations. Drug Discov Today 2006, 11, 580–594.
  • Krissinel, E. Crystal contacts as nature’s docking solutions. J Comput Chem 2009, 31, 133–143.
  • Clarke’s Analysis of Drugs and Poisons, © Pharmaceutical Press, Monographs, 2005.
  • Senem S A, Yüksel A, Nurullah S, Güleren A, Jose L B. Solvent Effects on pKa values of some substituted sulfonamides in acetonitrile–water binary mixtures by the UV-spectroscopy method. J Chem Eng Data 2009, 54, 3014–3021.

Reprints and Corporate Permissions

Please note: Selecting permissions does not provide access to the full text of the article, please see our help page How do I view content?

To request a reprint or corporate permissions for this article, please click on the relevant link below:

Academic Permissions

Please note: Selecting permissions does not provide access to the full text of the article, please see our help page How do I view content?

Obtain permissions instantly via Rightslink by clicking on the button below:

If you are unable to obtain permissions via Rightslink, please complete and submit this Permissions form. For more information, please visit our Permissions help page.