Novel quinazolinone-based 2,4-thiazolidinedione-3-acetic acid derivatives as potent aldose reductase inhibitors

Papers of special note have been highlighted as: • of interest; •• of considerable interest

References

• 1 Diabetes Atlas. Gan D (Ed.). International Diabetes Federation, Brussels, Belgium (2003).
  Google Scholar
• 2 Zimmet P, Alberti K, Shaw J. Global and societal implications of the diabetes epidemic. Nature 414, 782–787 (2001).
  Medline CASGoogle Scholar
• 3 Jain S, Saraf S. Type 2 diabetes mellitus – Its global prevalence and therapeutic strategies. Diabetes Metab. Syndr. Clin. Res. Rev. 4, 48–56 (2010).
  Google Scholar
• 4 Bjork S. The cost of diabetes and diabetes care. Diabetes Res. Clin. Pract. 54, S13–S18 (2001). • Highlights the healthcare expenditure on managing diabetic complications.
  MedlineGoogle Scholar
• 5 Lee AY, Chung SK, Chung SS. Demonstration that polyol accumulation is responsible for diabetic cataract by use of transgenic mice expressing the aldose reductase gene in the lens. Proc. Natl Acad. Sci. USA 92, 2780–2784 (1995).
  Medline CASGoogle Scholar
• 6 Brownlee M. Biochemistry and molecular cell biology of diabetic complications. Nature 414, 813–820 (2001).
  Medline CASGoogle Scholar
• 7 Srivastava S, Ramana K, Bhatnagar A. Role of aldose reductase and oxidative damage in diabetes and the consequent potential for therapeutic options. Endocr. Rev. 26, 380–392 (2005).
  Medline CASGoogle Scholar
• 8 Ramana K, Friedrich B, Srivastava S, Bhatnagar A, Srivastava S. Activation of nuclear factor-kappa B by hyperglycemia in vascular smooth muscle cells is regulated by aldose reductase. Diabetes 53, 2910–2920 (2004).
  Medline CASGoogle Scholar
• 9 Ramana K, Friedrich B, Tammali R, West M, Bhatnagar A, Srivastava S. Requirement of aldose reductase for the hyperglycemic activation of protein kinase C and formation of diacylglycerol in vascular smooth muscle cells. Diabetes 54, 818 (2005).
  Medline CASGoogle Scholar
• 10 Ramana K, Srivastava S. Mediation of aldose reductase in lipopolysaccharide-induced inflammatory signals in mouse peritoneal macrophages. Cytokine 36, 115–122 (2006).
  Medline CASGoogle Scholar
• 11 Tang W, Martin K, Hwa J. Aldose reductase, oxidative stress, and diabetic mellitus. Front Pharmacol. 3(87), 1–8 (2012).
  Medline CASGoogle Scholar
• 12 Costantino L, Rastelli G, Cignarella G, Vianello P, Barlocco D. New aldose reductase inhibitors as potential agents for the prevention of long-term diabetic complications. Exp. Opin. Ther. Patents 7, 843–858 (1997).
  CASGoogle Scholar
• 13 Yabe-Nishimura C. Aldose reductase in glucose toxicity: a potential target for the prevention of diabetic complications. Pharmacol. Rev. 50, 21–33 (1998).
  Medline CASGoogle Scholar
• 14 Suzen S, Buyukbingol E. Recent studies of aldose reductase enzyme inhibition for diabetic complications. Curr. Med. Chem. 10, 1329–1352 (2003).
  Medline CASGoogle Scholar
• 15 Oates P. Polyol pathway and diabetic peripheral neuropathy. Int. Rev. Neurobiol. 50, 325–392 (2002).
  Medline CASGoogle Scholar
• 16 El-Kabbani O, Ruiz F, Darmanin C, Chung R. Aldose reductase structures: implications for mechanism and inhibition. Cell. Mol. Life Sci. 61, 750–762 (2004).
  Medline CASGoogle Scholar
• 17 Ishibashi Y, Matsui T, Matsumoto T, Kato H, Yamagishi S. Ranirestat has a stronger inhibitory activity on aldose reductase and suppresses inflammatory reactions in high glucose-exposed endothelial cells. Diab. Vasc. Dis. Res. 13, 312–315 (2016).
  Medline CASGoogle Scholar
• 18 Kao Y, Donahue K, Chan A, Knight J, Silink M. A novel polymorphism in the aldose reductase gene promoter region is strongly associated with diabetic retinopathy in adolescents with Type I diabetes. Diabetes 48, 1338–1340 (1999).
  Medline CASGoogle Scholar
• 19 Heesom A, Hibberd M, Millward A, Demaine A. Polymorphism in the 50-end of the aldose reductase gene is strongly associated with the development of diabetic nephropathy in Type I diabetes. Diabetes 46, 287–291 (1997).
  Medline CASGoogle Scholar
• 20 Moczulski D, Burak W, Doria A, Zychma M, Zukowska-Szczechowska E, Grzeszczak W. The role of aldose reductase gene in the susceptibility to diabetic nephropathy in Type II (non-insulin-dependent) diabetes mellitus. Diabetologia 42, 94–97 (1999).
  Medline CASGoogle Scholar
• 21 Oates P, Mylari B. Aldose reductase inhibitors: therapeutic implications for diabetic complications. Expert Opin. Inv. Drug 8, 1–15 (1999).
  MedlineGoogle Scholar
• 22 Yamagishi M, Yamada Y, Ozaki K et al. Biological activities and quantitative structure–activity relationships of spiro[imidazolidine-4,4′(1′H)-quinazoline]-2,2′,5(3′H)-triones as aldose reductase inhibitors. J. Med. Chem. 35, 2085–2094 (1992).
  Medline CASGoogle Scholar
• 23 Kotani T, Nagaki Y, Ishii A et al. Highly selective aldose reductase inhibitors. 3. Structural diversity of 3-(arylmethyl)-2,4,5-trioxoimidazolidine-1-acetic acids. J. Med. Chem. 40, 684–694 (1997).
  Medline CASGoogle Scholar
• 24 Mylari B, Armento S, Beebe D et al. A novel series of non-carboxylic acid, non-hydantoin inhibitors of aldose reductase with potent oral activity in diabetic rat models: 6-(5-chloro-3-methylbenzofuran-2-sulfonyl)-2H-pyridazin-3-one and congeners. J. Med. Chem. 48, 6326–6339 (2005).
  Medline CASGoogle Scholar
• 25 Da Settimo F, Primofiore G, La Motta C et al. Naphtho[1, 2-d]isothiazoleacetic acid derivativesas a novelclass of selective aldose reductase inhibitors. J. Med. Chem. 48, 6897–6907 (2005).
  Medline CASGoogle Scholar
• 26 La Motta C, Sartini S, Salerno S et al. Acetic acid aldose reductase inhibitors bearing a five-membered heterocyclic core with potent topical activity in a visual impairment rat model. J. Med. Chem. 51, 3182–3193 (2008).
  Medline CASGoogle Scholar
• 27 Van Zandt M, Doan B, Sawicki D, Sredy J, Podjarny A. Discovery of [3-(4,5,7-trifluoro-benzothiazol-2-ylmethyl)-pyrrolo[2,3-b]pyridin-1-yl]acetic acids as highly potent and selective inhibitors of aldose reductase for treatment of chronic diabetic complications. Bioorg. Med. Chem. Lett. 19, 2006–2008 (2009).
  Medline CASGoogle Scholar
• 28 Ohmura C, Watada H, Azuma K et al. Aldose reductase inhibitor, epalrestat, reduces lipid hydroperoxides in Type 2 diabetes. Endocr. J. 56, 149–156 (2009).
  Medline CASGoogle Scholar
• 29 Del Corso A, Cappiello M, Mura U. From a dull enzyme to something else: facts and perspectives regarding aldose reductase. Curr. Med. Chem. 15, 1452–1461 (2008).
  Medline CASGoogle Scholar
• 30 Stefek M, Soltesova P, Majekova M, Rechlin C, Heine A, Klebe G. Identification of novel aldose reductase inhibitors based on carboxymethylated mercaptotriazinoindole scaffold. J. Med. Chem. 58, 2649–2657 (2015).
  Medline CASGoogle Scholar
• 31 Maccari R, Ottanà R. Targeting aldose reductase for the treatment of diabetes complications and inflammatory diseases: new insights and future directions. J. Med. Chem. 58, 2047–2067 (2015). •• Reviews the implication of aldose reductase inhibitors in both diabetic complications and inflammatory disorders.
  Medline CASGoogle Scholar
• 32 Chatzopoulou M, Pegklidou K, Papastavrou N, Demopoulos V. Development of aldose reductase inhibitors for the treatment of inflammatory disorders. Expert Opin. Drug Discov. 8, 1365–1380 (2013).
  Medline CASGoogle Scholar
• 33 Grewal A, Bhardwaj S, Pandita D, Lather V, Sekhon B. Updates on aldose reductase inhibitors for management of diabetic complications and non-diabetic diseases. Mini Rev. Med. Chem. 16, 120–162 (2016).
  Medline CASGoogle Scholar
• 34 Banditelli S, Boldrini E, Vilardo P et al. A new approach against sugar cataract through aldose reductase Inhibitors. Exp. Eye Res. 69, 533–538 (1999).
  Medline CASGoogle Scholar
• 35 Hotta N, Toyota T, Matsuoka K et al. Clinical efficacy of fidarestat, a novel aldose reductase inhibitor, for diabetic peripheral neuropathy. Diabetes Care 24, 1776–1782 (2001).
  Medline CASGoogle Scholar
• 36 Asano T, Saito Y, Kawakami M, Yamada N. Fidarestat (SNK-860) a potent aldose reductase inhibitor, normalizes the elevated sorbitol accumulation in erythrocytes of diabetic patients. J. Diabet. Complicat. 16, 133–138 (2002).
  Google Scholar
• 37 Okayama N, Omi H, Okouchi M et al. Mechanisms of inhibitory activity of the aldose reductase inhibitor, Epalrestat, on high glucose-mediated endothelial injury: neutrophil-endothelial cell adhesion and surface expression of endothelial adhesion molecules. J. Diabet. Complicat. 16, 321–326 (2002).
  Google Scholar
• 38 Nakahara M, Miyata K, Otani S et al. A randomised placebo controlled clinical trial of the aldose reducatse inhibitor CT-112 as management of corneal epithelial disorders in diabetic patients. Br. J. Ophthalm. 89, 266–268 (2005).
  Medline CASGoogle Scholar
• 39 Hotta N, Akanuma Y, Kawamori R et al. Long-term clinical effects of epalrestat, an aldose reductase inhibitor, on diabetic peripheral neuropathy. Diabetes Care 29, 1538–1544 (2006). • Highlights the mild and tolerable side effects of epalrestat.
  Medline CASGoogle Scholar
• 40 Oyama T, Miyasita Y, Watanabe H, Shirai K. The role of polyol pathway in high glucose-induced endothelial cell damages. Diabetes Res. Clin. Pract. 73, 227–234 (2006).
  Medline CASGoogle Scholar
• 41 Lorenzi M. The polyol pathway as a mechanism for diabetic retinopathy: attractive, elusive, and resilient. Exp. Diabetes Res. 2007, 61038 (2007).
  MedlineGoogle Scholar
• 42 Matsumoto T, Ono Y, Kurono M, Kuromiya A, Nakamura K, Bril V. Ranirestat (AS-3201) a potent aldose reductase inhibitor, reduces sorbinil levels and improves motor nerve conduction velocity in streptozotocin-diabetes rats. J. Pharmacol. Sci. 107, 231–237 (2008).
  Medline CASGoogle Scholar
• 43 Schemmel K, Padiyara R, D'Souza J. Aldose reductase inhibitors in the treatment of diabetic peripheral neuropathy: a review. J. Diabet. Complicat. 24, 354–360 (2010).
  Google Scholar
• 44 Bozdağ-Dündar O, Evranos B, Daş-Evcimen N, Sarikaya M, Ertan R. Synthesis and aldose reductase inhibitory activity of some new chromonyl-2,4-thiazolidinediones. Eur. J. Med. Chem. 43, 2412–2417 (2008).
  MedlineGoogle Scholar
• 45 Daş-Evcimen N, Bozdağ-Dündar O, Sarikaya M, Ertan R. In vitro aldose reductase inhibitory activity of some flavonyl-2,4-thiazolidinediones. J. Enzyme Inhib. Med. Chem. 3, 297–301 (2008).
  Google Scholar
• 46 Bozdag-Dundar O, Evcimen M, Ceylan-Unlusoy M, Rahmiye E, Mutlu S. Some new thiazolyl thiazolidinedione derivatives as aldose reductase inhibitors. Med. Chem. Res. 16, 39–47 (2007).
  CASGoogle Scholar
• 47 Sambasivarao S, Soni L, Gupta A, Hanumantharao P, Kaskhedikar S. Quantitative structure–activity analysis of 5-arylidene-2,4-thiazolidinediones as aldose reductase inhibitors. Bioorg. Med. Chem. Lett. 16, 512–520 (2006).
  Medline CASGoogle Scholar
• 48 Maccari R, Ottanà R, Curinga C et al. Structure–activity relationships and molecular modelling of 5-arylidene-2,4-thiazolidinediones active as aldose reductase inhibitors. Bioorg. Med. Chem. 13, 2809–2823 (2005).
  Medline CASGoogle Scholar
• 49 Rakowitz D, Maccari R, Ottanà R, Vigorita M. In vitro aldose reductase inhibitory activity of 5-benzyl-2,4-thiazolidinediones. Bioorg. Med. Chem. 14, 567–574 (2006).
  Medline CASGoogle Scholar
• 50 Maccari R, Ottanà R, Ciurleo R et al. Synthesis, induced-fit docking investigations, and in vitro aldose reductase inhibitory activity of non-carboxylic acid containing 2,4-thiazolidinedione derivatives. Bioorg. Med. Chem. 16, 5840–5852 (2008).
  Medline CASGoogle Scholar
• 51 Maccari R, Ciurleo R, Giglio M et al. Identification of new non-carboxylic acid containing inhibitors of aldose reductase. Bioorg. Med. Chem. 18, 4049–4055 (2010).
  Medline CASGoogle Scholar
• 52 Maccari R, Ottanà R, Ciurleo R et al. Evaluation of in vitro aldose redutase inhibitory activity of 5-arylidene-2,4-thiazolidinediones. Bioorg. Med. Chem. Lett. 17, 3886–3893 (2007).
  Medline CASGoogle Scholar
• 53 Zentgraf M, Steuber H, Koch C et al. How reliable are current docking approaches for structure-based drug design? Lessons from aldose reductase. Angew. Chem. Int. Ed. Engl. 46, 3575–3578 (2007).
  Medline CASGoogle Scholar
• 54 Steuber H, Zentgraf M, La Motta C, Sartini S, Heine A, Klebe G. Evidence for a novel binding site conformer of aldose reductase in ligand-bound state. J. Mol. Biol. 369, 186–197 (2007).
  Medline CASGoogle Scholar
• 55 Metwally K, Pratsinis H, Kletsas D. Novel 2, 4-thiazolidinediones: synthesis, in vitro cytotoxic activity, and mechanistic investigation. Eur. J. Med. Chem. 133, 340–350 (2017).
  Medline CASGoogle Scholar
• 56 Del-Corso A, Balestri F, Di Bugno E et al. A new approach to control the enigmatic activity of aldose reductase. PLoS ONE 8, e74076 (2013).
  Medline CASGoogle Scholar
• 57 Ramunno A, Cosconati S, Sartini S et al. Progresses in the pursuit of aldose reductase inhibitors: the structure-based lead optimization step. Eur. J. Med. Chem. 5, 216–26 (2012).
  Google Scholar
• 58 Sartini S, Cosconati S, Marinelli L et al. Benzofuroxane derivatives as multi-effective agents for the treatment of cardiovascular diabetic complications. Synthesis, functional evaluation, and molecular modeling studies. J. Med. Chem. 55, 10523–10531 (2012).
  Medline CASGoogle Scholar
• 59 Trott O, Olson A. AutoDock Vina: improving the speed and accuracy of docking with a new scoring function, efficient optimization, and multithreading. J. Comput. Chem. 31, 455–461 (2010).
  Medline CASGoogle Scholar
• 60 Morris G, Huey R, Lindstrom W et al. AutoDock4 and AutoDockTools4: automated docking with selective receptor flexibility. J. Comput. Chem. 30, 2785–2791 (2009).
  Medline CASGoogle Scholar
• 61 Howard E, Sanishvili R, Cachau R et al. Ultrahigh resolution drug design I: details of interactions in human aldose reductase-inhibitor complex at 0.66 A. Proteins 55, 792–804 (2004).
  Medline CASGoogle Scholar
• 62 Van Zandt M, Sibley E, McCann E et al. Design and synthesis of highly potent and selective (2-arylcarbamoyl-phenoxy)-acetic acid inhibitors of aldose reductase for treatment of chronic diabetic complications. Bioorg. Med. Chem. 12, 5661–5675 (2004).
  Medline CASGoogle Scholar
• 63 Wang L, Gu Q, Zheng X et al. Discovery of new selective human aldose reductase inhibitors through virtual screening multiple binding pocket conformations. J. Chem. Inf. Model 53, 2409–2422 (2013).
  Medline CASGoogle Scholar
• 64 Cosconati S, Forli S, Perryman A, Harris R, Goodsell D, Olson A. Virtual screening with AutoDock: theory and practice. Expert Opin. Drug Discov. 5, 597–607 (2010).
  Medline CASGoogle Scholar
• 65 Sanner M. The python interpreter as a framework for integrating scientific computing software-components. Scripps Res. Inst. 26, 1–12 (2008).
  Google Scholar
• 66 Case D, Cheatham T, Darden T et al. The amber biomolecular simulation programs. J. Comput. Chem. 26, 1668–1688 (2005).
  Medline CASGoogle Scholar
• 67 Lindorff-Larsen K, Piana S, Palmo K et al. Improved side-chain torsion potentials for the Amber ff99SB protein force field. Proteins 78, 1950–1958 (2010).
  Medline CASGoogle Scholar
• 68 Hanwell M, Curtis D, Lonie D, Vandermeersch T, Zurek E, Hutchison G. Avogadro: an advanced semantic chemical editor, visualization, and analysis platform. J. Chem. inform. 4, 17 (2012).
  CASGoogle Scholar
• 69 Wang J, Wolf R, Caldwell J, Kollman P, Case D. Development and testing of a general amber force field. J. Comput. Chem. 25, 1157–1174 (2004).
  Medline CASGoogle Scholar
• 70 Jorgensen W, Chandrasekhar J, Madura J, Impey R, Klein M. Comparison of simple potential functions for simulating liquid water. J. Chem. Phys. 79, 926–935 (1983).
  CASGoogle Scholar
• 71 Essmann U, Perera L, Berkowitz M, Darden T, Lee H, Pedersen L. A smooth particlemesh Ewald method. J. Chem. Phys. 103, 8577–8593 (1995).
  CASGoogle Scholar
• 72 Grest G, Kremer K. Molecular dynamics simulation for polymers in the presence of a heat bath. Phys. Rev. A Gen. Phys. 33, 3628–3631 (1986).
  Medline CASGoogle Scholar
• 73 Berendsen H, Postma J, van Gunsteren W, DiNola A, Haak J. Molecular dynamics with coupling to an external bath. J. Chem. Phys. 81, 3684–3690 (1984).
  CASGoogle Scholar
• 74 Ryckaert J, Ciccotti G, Berendsen H. Numerical integration of the cartesian equations of motion of a system with constraints: molecular dynamics of n-alkanes. J. Comput. Phys. 23, 327–341 (1977).
  CASGoogle Scholar
• 75 Pettersen E, Goddard T, Huang C et al. UCSF Chimera–a visualization system for exploratory research and analysis. J. Comput. Chem. 25, 1605–1612 (2004).
  Medline CASGoogle Scholar
• 76 Wriggers W, Schulten K. Protein domain movements: detection of rigid domains and visualization of hinges in comparisons of atomic coordinates. Proteins 29, 1–14 (1997).
  Medline CASGoogle Scholar
• 77 Laskowski R, Swindells M. LigPlot+: multiple ligand-protein interaction diagrams for drug discovery. J. Chem. Inf. Model 51, 2778–2786 (2011).
  Medline CASGoogle Scholar
• 78 Kollman A, Massova I, Reyes C et al. Calculating structures and free energies of complex molecules: combining molecular mechanics and continuum models. Acc. Chem. Res. 33, 889–897 (2000).
  Medline CASGoogle Scholar
• 79 Tsui V, Case D. Theory and applications of the generalized born solvation model in macromolecular simulations. Biopolymers 56, 275–291 (2000).
  Medline CASGoogle Scholar
• 80 Onufriev A, Bashford D, Case D. Modification of the generalized born model suitable for macromolecules. J. Phys. Chem. B 104, 3712–3720 (2000).
  CASGoogle Scholar
• 81 Domanig F. Synthese und einige Reaktionen yon 2-Azidomethyl-3-aryl-4-chinazolinonen. Monatshefte fur Chemie 112, 1195–1202 (1981).
  CASGoogle Scholar
• 82 Fetter J, Czuppon T, Hornyak G, Feller A. The synthesis of some 3-amino-2-halomethyl-, 2- halomethyl-3-(subst.amino)- and 2-halomethyl-3-hetarylquinazolin-4(3)-ones as potential plant protecting agents. Tetrahedron 47, 9393–9410 (1991).
  CASGoogle Scholar
• 83 Tani J, Yamada Y, Oine T, Ochiai T, Ishida R, Inoue I. Studies on biologically active halogenated compounds. 1. Synthesis and central nervous system depressant activity of 2- (fluoromethyl)-3-aryl-4(3H)-quinazolinone derivatives. J. Med. Chem. 22, 95–99 (1979).
  Medline CASGoogle Scholar
• 84 Giri R, Thaker H, Giordano T et al. Design, synthesis and evaluation of novel 2- thiophen-5-yl-3H-quinazolin-4-one analogues as inhibitors of transcription factors NfkappaB and AP-1 mediated transcriptional activation: their possible utilization as antiinflammatory and anti-cancer agents. Bioorg. Med. Chem. 18, 2796–2808 (2010).
  Medline CASGoogle Scholar
• 85 Hymavati V, Sobhia M. Implication of crystal water molecules in inhibitor binding at ALR2 active site. Comput. Math. Methods Med. 2012, 541594 (2012).
  Medline CASGoogle Scholar
• 86 Adcock S, McCammon J. Molecular dynamics: survey of methods for simulating the activity of proteins. Chem. Rev. 106, 1589–1615 (2006).
  Medline CASGoogle Scholar