Multifunctional Hybrid Sulfonamides as Novel Therapeutic Agents for Alzheimer’s Disease

References

• Prince M , BryceR, AlbaneseE, WimoA, RibeiroW, FerriCP. The global prevalence of dementia: a systematic review and metaanalysis. Alzheimers Dement.9(1), 63.e2–75.e2 (2013).
   Web of Science ®Google Scholar
• Auld DS , KornecookTJ, BastianettoS, QuirionR. Alzheimer’s disease and the basal forebrain cholinergic system: relations to β-amyloid peptides, cognition, and treatment strategies. Prog. Neurobiol.68(3), 209–245 (2002).
   PubMed Web of Science ®Google Scholar
• Inestrosa NC , AlvarezA, PerezCAet al. Acetylcholinesterase accelerates assembly of amyloid-β-peptides into Alzheimer's fibrils: possible role of the peripheral site of the enzyme. Neuron16(4), 881–891 (1996).
   PubMed Web of Science ®Google Scholar
• Ganeshpurkar A , SwethaR, KumarDet al. Protein–protein interaction and aggregation inhibitors in Alzheimer's disease. Curr. Top. Med. Chem.19(7), 501–533 (2019).
   PubMed Web of Science ®Google Scholar
• Hardy J , SelkoeDJ. The amyloid hypothesis of Alzheimer’s disease: progress and problems on the road to therapeutics. Science297(5580), 353–356 (2002).
   PubMed Web of Science ®Google Scholar
• Haass C , SelkoeDJ. Soluble protein oligomers in neurodegeneration: lessons from the Alzheimer’s amyloid β-peptide. Nat. Rev. Mol. Cell Biol.8(2), 101–112 (2007).
   PubMed Web of Science ®Google Scholar
• Ittner LM , GötzJ. Amyloid-β and tau – a toxic pas de deux in Alzheimer’s disease. Nat. Rev. Neurosci.12(2), 67–72 (2011).
   Web of Science ®Google Scholar
• Bloom GS . Amyloid-β and tau: the trigger and bullet in Alzheimer disease pathogenesis. JAMA Neurol.71(4), 505–508 (2014).
   PubMed Web of Science ®Google Scholar
• Kumar D , GaneshpurkarA, KumarD, ModiGP, GuptaSK, SinghSK. Secretase inhibitors for the treatment of Alzheimer’s disease: long road ahead. Eur. J. Med. Chem.148, 436–452 (2018).
   PubMed Web of Science ®Google Scholar
• Knowles TP , VendruscoloM, DobsonCM. The amyloid state and its association with protein misfolding diseases. Nat. Rev. Mol. Cell Biol.15(6), 384 (2014).
   PubMed Web of Science ®Google Scholar
• Savelieff MG , LeeS, LiuY, LimMH. Untangling amyloid-β, tau, and metals in Alzheimer’s disease. ACS Chem. Biol.8(5), 856–865 (2013).
   PubMed Web of Science ®Google Scholar
• Rajasekhar K , MehtaK, GovindarajuT. Hybrid multifunctional modulators inhibit multifaceted Aβ toxicity and prevent mitochondrial damage. ACS Chem. Neurosci.9(6), 1432–1440 (2018).
   PubMed Web of Science ®Google Scholar
• Yong VW , ForsythPA, BellR, KrekoskiCA, EdwardsDR. Matrix metalloproteinases and diseases of the CNS. Trends Neurosci.21(2), 75–80 (1998).
   PubMed Web of Science ®Google Scholar
• Rosenberg GA . Matrix metalloproteinases and their multiple roles in neurodegenerative diseases. Lancet Neurol.8(2), 205–216 (2009).
   PubMed Web of Science ®Google Scholar
• Lorenzl S , AlbersD, LewittPet al. Tissue inhibitors of matrix metalloproteinases are elevated in cerebrospinal fluid of neurodegenerative diseases. J. Neurol. Sci.207(1), 71–76 (2003).
   PubMed Web of Science ®Google Scholar
• Brkic M , BalusuS, Van WonterghemEet al. Amyloid β oligomers disrupt blood–CSF barrier integrity by activating matrix metalloproteinases. J. Neurosci.35(37), 12766–12778 (2015).
   PubMed Web of Science ®Google Scholar
• Swetha R , GayenC, KumarD, SinghTD, ModiG, SinghSK. Biomolecular basis of matrix metallo proteinase-9 activity. Future Med. Chem.10(9), 1093–1112 (2018).
   PubMed Web of Science ®Google Scholar
• Saravanan C , SinghSK. Status of research on MMPs in India. Expert Opin. Ther. Tar.15(6), 715–728 (2011).
   PubMed Web of Science ®Google Scholar
• Kumar D , KumarM, SaravananC, SinghSK. Curcumin: a potential candidate for matrix metalloproteinase inhibitors. Expert Opin. Ther. Tar.16(10), 959–972 (2012).
   PubMed Web of Science ®Google Scholar
• Nordberg A , BallardC, BullockR, Darreh-ShoriT, SomogyiM. A review of butyrylcholinesterase as a therapeutic target in the treatment of Alzheimer’s disease. Prim. Care Companion CNS Disord.15(2), doi:10.4088/PCC.12r01412 (2013).
   PubMedGoogle Scholar
• Unzeta M , EstebanG, BoleaIet al. Multi-target directed donepezil-like ligands for Alzheimer's disease. Front. Neurosci.10, 205 (2016).
   PubMed Web of Science ®Google Scholar
• Huggins DJ , ShermanW, TidorB. Rational approaches to improving selectivity in drug design. J. Med. Chem.55(4), 1424–1444 (2012).
   PubMed Web of Science ®Google Scholar
• Wei D , JiangX, ZhouLet al. Discovery of multitarget inhibitors by combining molecular docking with common pharmacophore matching. J. Med. Chem.51(24), 7882–7888 (2008).
   PubMed Web of Science ®Google Scholar
• Prati F , CavalliA, BolognesiMJM. Navigating the chemical space of multitarget-directed ligands: from hybrids to fragments in Alzheimer’s disease. Molecules21(4), 466 (2016).
   PubMed Web of Science ®Google Scholar
• Cavalli A , BolognesiML, MinariniAet al. Multi-target-directed ligands to combat neurodegenerative diseases. J. Med. Chem.51(3), 347–372 (2008).
   PubMed Web of Science ®Google Scholar
• Zemek F , DrtinovaL, NepovimovaEet al. Outcomes of Alzheimer’s disease therapy with acetylcholinesterase inhibitors and memantine. Expert Opin. Drug Saf.13(6), 759–774 (2014).
   PubMed Web of Science ®Google Scholar
• Panek D , WięckowskaA, JończykJet al. Design, synthesis, and biological evaluation of 1-benzylamino-2-hydroxyalkyl derivatives as new potential disease-modifying multifunctional anti-Alzheimer’s agents. ACS Chem. Neurosci.9(5), 1074–1094 (2018).
   PubMed Web of Science ®Google Scholar
• Prati F , BergaminiC, FatoRet al. Novel 8‐hydroxyquinoline derivatives as multitarget compounds for the treatment of Alzheimer’s disease. ChemMedChem11(12), 1284–1295 (2016).
   PubMed Web of Science ®Google Scholar
• Więckowska A , WichurT, GodyńJet al. Novel multitarget-directed ligands aiming at symptoms and causes of Alzheimer’s disease. ACS Chem. Neurosci.9(5), 1195–1214 (2018).
   PubMed Web of Science ®Google Scholar
• Kumar D , GuptaSK, GaneshpurkarAet al. Development of piperazinediones as dual inhibitor for treatment of Alzheimer’s disease. Eur. J. Med. Chem.150, 87–101 (2018).
   PubMed Web of Science ®Google Scholar
• Kumar D , GuptaSK, GaneshpurkarAet al. Biological profiling of piperazinediones for the management of anxiety. Pharmacol. Biochem. Behav.176, 63–71 (2019).
   PubMed Web of Science ®Google Scholar
• Rajasekhar K , MadhuC, GovindarajuT. Natural tripeptide-based inhibitor of multifaceted amyloid β toxicity. ACS Chem. Neurosci.7(9), 1300–1310 (2016).
   PubMed Web of Science ®Google Scholar
• Jan A , HartleyDM, LashuelHA. Preparation and characterization of toxic Aβ aggregates for structural and functional studies in Alzheimer’s disease research. Nat. Protoc.5(6), 1186 (2010).
   PubMed Web of Science ®Google Scholar
• Vyas NA , SinghSB, KumbharASet al. Acetylcholinesterase and Aβ aggregation inhibition by heterometallic ruthenium (II)–platinum (II) polypyridyl complexes. Inorg. Chem.57(13), 7524–7535 (2018).
   PubMed Web of Science ®Google Scholar
• Satheeshkumar S , MohammadFaizan B, AshokK, GopalN, SushilKumar S. Design, synthesis and biological evaluation of carbazole derivatives as antitubercular and antibacterial agents. Curr. Bioact. Compd.14, 1–15 (2018).
   Google Scholar
• Revilla S , UrsuletS, Álvarez‐LópezMJet al. Lenti‐GDNF gene therapy protects against Alzheimer’s disease‐like neuropathology in 3×Tg‐AD mice and MC65 cells. CNS Neurosci. Ther.20(11), 961–972 (2014).
   PubMed Web of Science ®Google Scholar
• Modi G , AntonioT, ReithM, DuttaA. Structural modifications of neuroprotective anti-Parkinsonian (−)-N 6-(2-(4-(Biphenyl-4-yl) piperazin-1-yl)-ethyl)-N 6-propyl-4, 5, 6, 7-tetrahydrobenzo [d] thiazole-2, 6-diamine (D-264): an effort toward the improvement of in vivo efficacy of the parent molecule. J. Med. Chem.57(4), 1557–1572 (2014).
   PubMed Web of Science ®Google Scholar
• Shidore M , MachhiJ, ShingalaKet al. Benzylpiperidine-linked diarylthiazoles as potential anti-Alzheimer’s agents: synthesis and biological evaluation. J. Med. Chem.59(12), 5823–5846 (2016).
   PubMed Web of Science ®Google Scholar
• Ganeshpurkar A , KumarD, SinghSK. Design, synthesis and collagenase inhibitory activity of some novel phenylglycine derivatives as metalloproteinase inhibitors. Int. J. Biol. Macromol.107, 1491–1500 (2018).
   PubMed Web of Science ®Google Scholar
• Umre R , GaneshpurkarA, GaneshpurkarAet al. In vitro, in vivo and in silico antiulcer activity of ferulic acid. Future J. Pharm. Sci.4(2), 248–253 (2018).
   Web of Science ®Google Scholar
• Lee S , LiuY, LiuY, LimMH. Untangling amyloid-β, Tau, and metals in Alzheimer’s disease. ACS Chem. Biol.8(5), 856–865 (2013).
   PubMed Web of Science ®Google Scholar
• Reybier K , AyalaS, AliesBet al. Free superoxide is an intermediate in the production of H2O2 by copper (I)‐Aβ peptide and O2. Angew Chem. Int. Ed. Engl.55(3), 1085–1089 (2016).
   PubMed Web of Science ®Google Scholar
• Lim P , HussJr A, EckertC. Oxidation of aqueous sulfur dioxide. 3. The effects of chelating agents and phenolic antioxidants. J. Phys. Chem. A86(21), 4233–4237 (1982).
   Web of Science ®Google Scholar
• Atmaca G . Antioxidant effects of sulfur-containing amino acids. Yonsei Med. J.45, 776–788 (2004).
   PubMed Web of Science ®Google Scholar
• Mensch J , OyarzabalJ, MackieC, AugustijnsP. In vivo, in vitro and in silico methods for small molecule transfer across the BBB. J. Pharm. Sci.98(12), 4429–4468 (2009).
   PubMed Web of Science ®Google Scholar
• Fiorito J , VendomeJ, SaeedFet al. Identification of a novel 1, 2, 3, 4-tetrahydrobenzo [b][1, 6] naphthyridine analogue as a potent phosphodiesterase 5 inhibitor with improved aqueous solubility for the treatment of Alzheimer’s disease. J. Med. Chem.60(21), 8858–8875 (2017).
   PubMed Web of Science ®Google Scholar