Research Article
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Year 2021, Volume 1, Issue 1, 56 - 64, 15.12.2021

Abstract

References

  • Airoldi, C., La Ferla, B., D'Orazio, G., Ciaramelli, C., Palmioli, A., 2018. Flavonoids in the treatment of Alzheimer's and other neurodegenerative diseases. Current Medicinal Chemistry, 25(27), 3228-3246.
  • Ali, M.Y., Jannat, S., Edraki, N., Das, S., Chang, W.K., Kim, H.C., Park, S.K., Chang, M.S., 2019. Flavanone glycosides inhibit β-site amyloid precursor protein cleaving enzyme 1 and cholinesterase and reduce Aβ aggregation in the amyloidogenic pathway. Chemico-Biological Interactions, 309, 108707.
  • Álvarez Rojas, A., Moreno Mauro, R.D., Garrido, J., 1996. Acetylcholinesterase Accelerates Assembly of Amyloid-B-Peptides Into Alzheimer's Fibrils: Possible Role of the Peripheral Site of the Enzyme. Neuron, 16(4), 881-891.
  • Anderson, J.P., Chen, Y., Kim, K.S., Robakis, N.K., 1992. An alternative secretase cleavage produces soluble Alzheimer amyloid precursor protein containing a potentially amyloidogenic sequence. Journal of Neurochemistry, 59(6), 2328-2331.
  • Burns, A., Iliffe, S., 2009. Alzheimer’s disease. BMJ 338, b158.
  • Carvajal, F.J., Inestrosa, N.C., 2011. Interactions of AChE with Aβ aggregates in Alzheimer’s brain: therapeutic relevance of IDN 5706. Frontiers in Molecular Neuroscience, 4, 19.
  • Chandran, U., Mehendale, N., Tillu, G., Patwardhan, B., 2015. Network Pharmacology of Ayurveda Formulation Triphala with Special Reference to Anti-Cancer Property. Comb Chem High Throughput Screen, 18(9), 846-854.
  • Daina, A., Michielin, O., Zoete, V., 2019. SwissTargetPrediction: updated data and new features for efficient prediction of protein targets of small molecules. Nucleic Acids Research, 47(W1), W357-W364.
  • Darvesh, S., Cash, M.K., Reid, G.A., Martin, E., Mitnitski, A., Geula, C., 2012. Butyrylcholinesterase is associated with β-amyloid plaques in the transgenic APPSWE/PSEN1dE9 mouse model of Alzheimer disease. Journal of Neuropathology & Experimental Neurology, 71(1), 2-14.
  • Dinamarca, M.C., Sagal, J.P., Quintanilla, R.A., Godoy, J.A., Arrázola, M.S., Inestrosa, N.C., 2010. Amyloid-β-Acetylcholinesterase complexes potentiate neurodegenerative changes induced by the Aβ peptide. Implications for the pathogenesis of Alzheimer's disease. Molecular Neurodegeneration, 5(1), 1-15.
  • Ferri, C.P., Prince, M., Brayne, C., Brodaty, H., Fratiglioni, L., Ganguli, M., Hall, K., Hasegawa, K., Hendrie, H., Huang, Y., 2005. Global prevalence of dementia: a Delphi consensus study. The Lancet, 366(9503), 2112-2117.
  • Francis, P.T., Palmer, A.M., Snape, M., Wilcock, G.K., 1999. The cholinergic hypothesis of Alzheimer’s disease: a review of progress. Journal of Neurology, Neurosurgery & Psychiatry, 66(2), 137-147.
  • Gabuzda, D., Busciglio, J., Chen, L.B., Matsudaira, P., Yankner, B.A., 1994. Inhibition of energy metabolism alters the processing of amyloid precursor protein and induces a potentially amyloidogenic derivative. Journal of Biological Chemistry, 269(18), 13623-13628.
  • Greig, N.H., Lahiri, D.K., Sambamurti, K., 2002. Butyrylcholinesterase: an important new target in Alzheimer's disease therapy. International Psychogeriatrics, 14(S1), 77-91.
  • Guzzi, C., Colombo, L., Luigi, A.D., Salmona, M., Nicotra, F., Airoldi, C., 2017. Flavonoids and Their Glycosides as Anti‐amyloidogenic Compounds: Aβ1–42 Interaction Studies to Gain New Insights into Their Potential for Alzheimer's Disease Prevention and Therapy. Chemistry–An Asian Journal, 12(1), 67-75.
  • Haass, C., Schlossmacher, M.G., Hung, A.Y., Vigo-Pelfrey, C., Mellon, A., Ostaszewski, B.L., Lieberburg, I., Koo, E.H., Schenk, D., Teplow, D.B., 1992. Amyloid β-peptide is produced by cultured cells during normal metabolism. Nature, 359(6393), 322-325.
  • Hanwell, M.D., Curtis, D.E., Lonie, D.C., Vandermeersch, T., Zurek, E., Hutchison, G.R., 2012. Avogadro: an open-source molecular builder and visualization tool. Journal of Cheminformatics, 4, 17.
  • Hardy, J., Allsop, D., 1991. Amyloid deposition as the central event in the aetiology of Alzheimer's disease. Trends in Pharmacological Sciences, 12, 383-388.
  • Hsu, F., Park, G., Guo, Z., 2018. Key residues for the formation of Aβ42 amyloid fibrils. ACS Omega, 3(7), 8401-8407.
  • Inestrosa, N.C., Sagal, J.P., Colombres, M., 2005. Acetylcholinesterase interaction with Alzheimer amyloid β. Alzheimer’s Disease, 38, 299-317.
  • Istifli, E.S., 2021. Chemical Composition, Antioxidant and Enzyme Inhibitory Activities of Onosma bourgaei and Onosma trachytricha and in Silico Molecular Docking Analysis of Dominant Compounds. Molecules, 26(10), 2981.
  • Istifli, E.S., Sihoglu Tepe, A., Sarikurkcu, C., Tepe, B., 2021. Investigation of molecular interactions between some hydroxybenzoic and hydroxycinnamic acids and the receptor binding site (RBD) of 2019-nCoV spike protein and host proteases [transmembrane protease, serin 2 (TMPRSS2), cathepsin B and cathepsin L] by in silico analysis. International Journal of Secondary Metabolite, 8(3), 246-271.
  • Li, B., Stribley, J.A., Ticu, A., Xie, W., Schopfer, L.M., Hammond, P., Brimijoin, S., Hinrichs, S.H., Lockridge, O., 2000. Abundant tissue butyrylcholinesterase and its possible function in the acetylcholinesterase knockout mouse. Journal of Neurochemistry, 75(3), 1320-1331.
  • Li, H., Robertson, A.D., Jensen, J.H., 2005. Very fast empirical prediction and rationalization of protein pKa values. Proteins, 61(4), 704-721.
  • Liu, F., Xu, K., Xu, Z., de Las Rivas, M., Wang, C., Li, X., Lu, J., Zhou, Y., Delso, I., Merino, P., 2017. The small molecule luteolin inhibits N-acetyl-α-galactosaminyltransferases and reduces mucin-type O-glycosylation of amyloid precursor protein. Journal of Biological Chemistry, 292(52), 21304-21319.
  • Nathan, C., Calingasan, N., Nezezon, J., Ding, A., Lucia, M.S., La Perle, K., Fuortes, M., Lin, M., Ehrt, S., Kwon, N.S., 2005. Protection from Alzheimer's-like disease in the mouse by genetic ablation of inducible nitric oxide synthase. Journal of Experimental Medicine, 202(9), 1163-1169.
  • O'Boyle, N.M., Banck, M., James, C.A., Morley, C., Vandermeersch, T., Hutchison, G.R., 2011. Open Babel: An open chemical toolbox. Journal of Cheminformatics, 3, 33.
  • Patil, C.S., Singh, V.P., Satyanarayan, P., Jain, N.K., Singh, A., Kulkarni, S.K., 2003. Protective effect of flavonoids against aging-and lipopolysaccharide-induced cognitive impairment in mice. Pharmacology, 69(2), 59-67.
  • Pires, D.E., Blundell, T.L., Ascher, D.B., 2015. pkCSM: Predicting Small-Molecule Pharmacokinetic and Toxicity Properties Using Graph-Based Signatures. Journal of Medicinal Chemistry, 58(9), 4066-4072.
  • Qin, L., Chen, Z., Yang, L., Shi, H., Wu, H., Zhang, B., Zhang, W., Xu, Q., Huang, F., Wu, X., 2019. Luteolin-7-O-glucoside protects dopaminergic neurons by activating estrogen-receptor-mediated signaling pathway in MPTP-induced mice. Toxicology, 426, 152256.
  • Salehi, B., Venditti, A., Sharifi-Rad, M., Kregiel, D., Sharifi-Rad, J., Durazzo, A., Lucarini, M., Santini, A., Souto, E.B., Novellino, E., Antolak, H., Azzini, E., Setzer, W.N., Martins, N., 2019. The Therapeutic Potential of Apigenin. International Journal of Molecular Sciences, 20(6).
  • Seubert, P., Oltersdorf, T., Lee, M.G., Barbour, R., Blomquist, C., Davis, D.L., Bryant, K., Fritz, L.C., Galasko, D., Thal, L.J., 1993. Secretion of β-amyloid precursor protein cleaved at the amino terminus of the β-amyloid peptide. Nature, 361(6409), 260-263.
  • Seubert, P., Vigo-Pelfrey, C., Esch, F., Lee, M., Dovey, H., Davis, D., Sinha, S., Schiossmacher, M., Whaley, J., Swindlehurst, C., 1992. Isolation and quantification of soluble Alzheimer's β-peptide from biological fluids. Nature, 359(6393), 325-327.
  • Spoerri, L., Vella, L.J., Pham, C.L., Barnham, K.J., Cappai, R., 2012. The amyloid precursor protein copper binding domain histidine residues 149 and 151 mediate APP stability and metabolism. Journal of Biological Chemistry, 287(32), 26840-26853.
  • Sun, X., Chen, W.-D., Wang, Y.-D., 2015. β-Amyloid: the key peptide in the pathogenesis of Alzheimer’s disease. Frontiers in Pharmacology, 6, 221.
  • Trott, O., Olson, A.J., 2010. AutoDock Vina: improving the speed and accuracy of docking with a new scoring function, efficient optimization, and multithreading. Journal of Computational Chemistry, 31(2), 455-461.
  • Tundis, R., Bonesi, M., Menichini, F., Loizzo, M.R., Conforti, F., Statti, G., Pirisi, F.M., Menichini, F., 2012. Antioxidant and anti-cholinesterase activity of Globularia meridionalis extracts and isolated constituents. Natural Product Communications, 7(8), 1934578X1200700814.
  • Valdes-Tresanco, M.S., Valdes-Tresanco, M.E., Valiente, P.A., Moreno, E., 2020. AMDock: a versatile graphical tool for assisting molecular docking with Autodock Vina and Autodock4. Biology Direct, 15(1), 12.
  • Zhao, L., Wang, J.-L., Liu, R., Li, X.-X., Li, J.-F., Zhang, L., 2013. Neuroprotective, anti-amyloidogenic and neurotrophic effects of apigenin in an Alzheimer’s disease mouse model. Molecules, 18(8), 9949-9965.

Assessment of apigenin-7-glucoside and luteolin-7-glucoside as multi-targeted agents against Alzheimer's disease: a molecular docking study

Year 2021, Volume 1, Issue 1, 56 - 64, 15.12.2021

Abstract

Although the incidence of Alzheimer's disease (AD) is increasing in society, unfortunately, no definite progress has been made in treating this disease yet. In this study, the potential of apigenin-7-glucoside (A7G) and luteolin-7-glucoside (L7G) to be used as multi-targeted agents in AD was investigated by molecular docking calculations against the acetylcholinesterase (AChE), butyrylcholinesterase (BChE), amyloid precursor protein (APP) and 42-residue beta-amyloid peptide (Aβ). A7G and L7G exhibited very high binding affinity (-9.42 and -9.60 kcal/mol for A7G; -9.30 and -9.90 kcal/mol for L7G) to AChE and BChE, respectively, while the affinities of these two flavonoid glycosides towards APP and Aβ peptide (-6.10 and -6.0 kcal/mol for A7G; -6.30 and -6.10 kcal/mol for L7G) were moderately strong. Compared to rivastigmine, A7G and L7G exhibited a highly significant binding affinity, even stronger than rivastigmine, for AChE and BChE. Although A7G showed a more drug-like physicochemical character than L7G, both ligands were within the normal range for ADMET and did not show high affinity for cellular proteins, according to the results of SwissTarget analysis. According to the STITCH interaction analysis, both ligands had the potential to inhibit enzymes predominantly in the inflammatory pathway (ADIPOQ, NOS1, NOS2 and NOS3). As a result, A7G and L7G exhibit multi-targeted agent properties in AD. Our results should also be verified by experimental enzyme inhibition studies, which may be performed simultaneously on AChE, BChE, APP, and Aβ peptides.

References

  • Airoldi, C., La Ferla, B., D'Orazio, G., Ciaramelli, C., Palmioli, A., 2018. Flavonoids in the treatment of Alzheimer's and other neurodegenerative diseases. Current Medicinal Chemistry, 25(27), 3228-3246.
  • Ali, M.Y., Jannat, S., Edraki, N., Das, S., Chang, W.K., Kim, H.C., Park, S.K., Chang, M.S., 2019. Flavanone glycosides inhibit β-site amyloid precursor protein cleaving enzyme 1 and cholinesterase and reduce Aβ aggregation in the amyloidogenic pathway. Chemico-Biological Interactions, 309, 108707.
  • Álvarez Rojas, A., Moreno Mauro, R.D., Garrido, J., 1996. Acetylcholinesterase Accelerates Assembly of Amyloid-B-Peptides Into Alzheimer's Fibrils: Possible Role of the Peripheral Site of the Enzyme. Neuron, 16(4), 881-891.
  • Anderson, J.P., Chen, Y., Kim, K.S., Robakis, N.K., 1992. An alternative secretase cleavage produces soluble Alzheimer amyloid precursor protein containing a potentially amyloidogenic sequence. Journal of Neurochemistry, 59(6), 2328-2331.
  • Burns, A., Iliffe, S., 2009. Alzheimer’s disease. BMJ 338, b158.
  • Carvajal, F.J., Inestrosa, N.C., 2011. Interactions of AChE with Aβ aggregates in Alzheimer’s brain: therapeutic relevance of IDN 5706. Frontiers in Molecular Neuroscience, 4, 19.
  • Chandran, U., Mehendale, N., Tillu, G., Patwardhan, B., 2015. Network Pharmacology of Ayurveda Formulation Triphala with Special Reference to Anti-Cancer Property. Comb Chem High Throughput Screen, 18(9), 846-854.
  • Daina, A., Michielin, O., Zoete, V., 2019. SwissTargetPrediction: updated data and new features for efficient prediction of protein targets of small molecules. Nucleic Acids Research, 47(W1), W357-W364.
  • Darvesh, S., Cash, M.K., Reid, G.A., Martin, E., Mitnitski, A., Geula, C., 2012. Butyrylcholinesterase is associated with β-amyloid plaques in the transgenic APPSWE/PSEN1dE9 mouse model of Alzheimer disease. Journal of Neuropathology & Experimental Neurology, 71(1), 2-14.
  • Dinamarca, M.C., Sagal, J.P., Quintanilla, R.A., Godoy, J.A., Arrázola, M.S., Inestrosa, N.C., 2010. Amyloid-β-Acetylcholinesterase complexes potentiate neurodegenerative changes induced by the Aβ peptide. Implications for the pathogenesis of Alzheimer's disease. Molecular Neurodegeneration, 5(1), 1-15.
  • Ferri, C.P., Prince, M., Brayne, C., Brodaty, H., Fratiglioni, L., Ganguli, M., Hall, K., Hasegawa, K., Hendrie, H., Huang, Y., 2005. Global prevalence of dementia: a Delphi consensus study. The Lancet, 366(9503), 2112-2117.
  • Francis, P.T., Palmer, A.M., Snape, M., Wilcock, G.K., 1999. The cholinergic hypothesis of Alzheimer’s disease: a review of progress. Journal of Neurology, Neurosurgery & Psychiatry, 66(2), 137-147.
  • Gabuzda, D., Busciglio, J., Chen, L.B., Matsudaira, P., Yankner, B.A., 1994. Inhibition of energy metabolism alters the processing of amyloid precursor protein and induces a potentially amyloidogenic derivative. Journal of Biological Chemistry, 269(18), 13623-13628.
  • Greig, N.H., Lahiri, D.K., Sambamurti, K., 2002. Butyrylcholinesterase: an important new target in Alzheimer's disease therapy. International Psychogeriatrics, 14(S1), 77-91.
  • Guzzi, C., Colombo, L., Luigi, A.D., Salmona, M., Nicotra, F., Airoldi, C., 2017. Flavonoids and Their Glycosides as Anti‐amyloidogenic Compounds: Aβ1–42 Interaction Studies to Gain New Insights into Their Potential for Alzheimer's Disease Prevention and Therapy. Chemistry–An Asian Journal, 12(1), 67-75.
  • Haass, C., Schlossmacher, M.G., Hung, A.Y., Vigo-Pelfrey, C., Mellon, A., Ostaszewski, B.L., Lieberburg, I., Koo, E.H., Schenk, D., Teplow, D.B., 1992. Amyloid β-peptide is produced by cultured cells during normal metabolism. Nature, 359(6393), 322-325.
  • Hanwell, M.D., Curtis, D.E., Lonie, D.C., Vandermeersch, T., Zurek, E., Hutchison, G.R., 2012. Avogadro: an open-source molecular builder and visualization tool. Journal of Cheminformatics, 4, 17.
  • Hardy, J., Allsop, D., 1991. Amyloid deposition as the central event in the aetiology of Alzheimer's disease. Trends in Pharmacological Sciences, 12, 383-388.
  • Hsu, F., Park, G., Guo, Z., 2018. Key residues for the formation of Aβ42 amyloid fibrils. ACS Omega, 3(7), 8401-8407.
  • Inestrosa, N.C., Sagal, J.P., Colombres, M., 2005. Acetylcholinesterase interaction with Alzheimer amyloid β. Alzheimer’s Disease, 38, 299-317.
  • Istifli, E.S., 2021. Chemical Composition, Antioxidant and Enzyme Inhibitory Activities of Onosma bourgaei and Onosma trachytricha and in Silico Molecular Docking Analysis of Dominant Compounds. Molecules, 26(10), 2981.
  • Istifli, E.S., Sihoglu Tepe, A., Sarikurkcu, C., Tepe, B., 2021. Investigation of molecular interactions between some hydroxybenzoic and hydroxycinnamic acids and the receptor binding site (RBD) of 2019-nCoV spike protein and host proteases [transmembrane protease, serin 2 (TMPRSS2), cathepsin B and cathepsin L] by in silico analysis. International Journal of Secondary Metabolite, 8(3), 246-271.
  • Li, B., Stribley, J.A., Ticu, A., Xie, W., Schopfer, L.M., Hammond, P., Brimijoin, S., Hinrichs, S.H., Lockridge, O., 2000. Abundant tissue butyrylcholinesterase and its possible function in the acetylcholinesterase knockout mouse. Journal of Neurochemistry, 75(3), 1320-1331.
  • Li, H., Robertson, A.D., Jensen, J.H., 2005. Very fast empirical prediction and rationalization of protein pKa values. Proteins, 61(4), 704-721.
  • Liu, F., Xu, K., Xu, Z., de Las Rivas, M., Wang, C., Li, X., Lu, J., Zhou, Y., Delso, I., Merino, P., 2017. The small molecule luteolin inhibits N-acetyl-α-galactosaminyltransferases and reduces mucin-type O-glycosylation of amyloid precursor protein. Journal of Biological Chemistry, 292(52), 21304-21319.
  • Nathan, C., Calingasan, N., Nezezon, J., Ding, A., Lucia, M.S., La Perle, K., Fuortes, M., Lin, M., Ehrt, S., Kwon, N.S., 2005. Protection from Alzheimer's-like disease in the mouse by genetic ablation of inducible nitric oxide synthase. Journal of Experimental Medicine, 202(9), 1163-1169.
  • O'Boyle, N.M., Banck, M., James, C.A., Morley, C., Vandermeersch, T., Hutchison, G.R., 2011. Open Babel: An open chemical toolbox. Journal of Cheminformatics, 3, 33.
  • Patil, C.S., Singh, V.P., Satyanarayan, P., Jain, N.K., Singh, A., Kulkarni, S.K., 2003. Protective effect of flavonoids against aging-and lipopolysaccharide-induced cognitive impairment in mice. Pharmacology, 69(2), 59-67.
  • Pires, D.E., Blundell, T.L., Ascher, D.B., 2015. pkCSM: Predicting Small-Molecule Pharmacokinetic and Toxicity Properties Using Graph-Based Signatures. Journal of Medicinal Chemistry, 58(9), 4066-4072.
  • Qin, L., Chen, Z., Yang, L., Shi, H., Wu, H., Zhang, B., Zhang, W., Xu, Q., Huang, F., Wu, X., 2019. Luteolin-7-O-glucoside protects dopaminergic neurons by activating estrogen-receptor-mediated signaling pathway in MPTP-induced mice. Toxicology, 426, 152256.
  • Salehi, B., Venditti, A., Sharifi-Rad, M., Kregiel, D., Sharifi-Rad, J., Durazzo, A., Lucarini, M., Santini, A., Souto, E.B., Novellino, E., Antolak, H., Azzini, E., Setzer, W.N., Martins, N., 2019. The Therapeutic Potential of Apigenin. International Journal of Molecular Sciences, 20(6).
  • Seubert, P., Oltersdorf, T., Lee, M.G., Barbour, R., Blomquist, C., Davis, D.L., Bryant, K., Fritz, L.C., Galasko, D., Thal, L.J., 1993. Secretion of β-amyloid precursor protein cleaved at the amino terminus of the β-amyloid peptide. Nature, 361(6409), 260-263.
  • Seubert, P., Vigo-Pelfrey, C., Esch, F., Lee, M., Dovey, H., Davis, D., Sinha, S., Schiossmacher, M., Whaley, J., Swindlehurst, C., 1992. Isolation and quantification of soluble Alzheimer's β-peptide from biological fluids. Nature, 359(6393), 325-327.
  • Spoerri, L., Vella, L.J., Pham, C.L., Barnham, K.J., Cappai, R., 2012. The amyloid precursor protein copper binding domain histidine residues 149 and 151 mediate APP stability and metabolism. Journal of Biological Chemistry, 287(32), 26840-26853.
  • Sun, X., Chen, W.-D., Wang, Y.-D., 2015. β-Amyloid: the key peptide in the pathogenesis of Alzheimer’s disease. Frontiers in Pharmacology, 6, 221.
  • Trott, O., Olson, A.J., 2010. AutoDock Vina: improving the speed and accuracy of docking with a new scoring function, efficient optimization, and multithreading. Journal of Computational Chemistry, 31(2), 455-461.
  • Tundis, R., Bonesi, M., Menichini, F., Loizzo, M.R., Conforti, F., Statti, G., Pirisi, F.M., Menichini, F., 2012. Antioxidant and anti-cholinesterase activity of Globularia meridionalis extracts and isolated constituents. Natural Product Communications, 7(8), 1934578X1200700814.
  • Valdes-Tresanco, M.S., Valdes-Tresanco, M.E., Valiente, P.A., Moreno, E., 2020. AMDock: a versatile graphical tool for assisting molecular docking with Autodock Vina and Autodock4. Biology Direct, 15(1), 12.
  • Zhao, L., Wang, J.-L., Liu, R., Li, X.-X., Li, J.-F., Zhang, L., 2013. Neuroprotective, anti-amyloidogenic and neurotrophic effects of apigenin in an Alzheimer’s disease mouse model. Molecules, 18(8), 9949-9965.

Details

Primary Language English
Subjects Pharmacology and Pharmacy
Journal Section Research Articles
Authors

Erman Salih İSTİFLİ (Primary Author)
Çukurova Üniversitesi
0000-0003-2189-0703
Türkiye


Cengiz SARIKÜRKCÜ
AFYONKARAHISAR HEALTH SCIENCES UNIVERSITY
0000-0001-5094-2520
Türkiye

Supporting Institution None
Project Number None
Publication Date December 15, 2021
Application Date July 31, 2021
Acceptance Date August 10, 2021
Published in Issue Year 2021, Volume 1, Issue 1

Cite

Bibtex @research article { ijpbp976969, journal = {International Journal of Plant Based Pharmaceuticals}, issn = {}, eissn = {2791-7509}, address = {Kilis 7 Aralık Üniversitesi, Fen-Edebiyat Fakültesi, Moleküler Biyoloji ve Genetik Bölümü, 79000, Merkez-KİLİS}, publisher = {Kilis 7 Aralik University}, year = {2021}, volume = {1}, pages = {56 - 64}, doi = {}, title = {Assessment of apigenin-7-glucoside and luteolin-7-glucoside as multi-targeted agents against Alzheimer's disease: a molecular docking study}, key = {cite}, author = {İstifli, Erman Salih and Sarıkürkcü, Cengiz} }
APA İstifli, E. S. & Sarıkürkcü, C. (2021). Assessment of apigenin-7-glucoside and luteolin-7-glucoside as multi-targeted agents against Alzheimer's disease: a molecular docking study . International Journal of Plant Based Pharmaceuticals , 1 (1) , 56-64 . Retrieved from https://dergipark.org.tr/en/pub/ijpbp/issue/64282/976969
MLA İstifli, E. S. , Sarıkürkcü, C. "Assessment of apigenin-7-glucoside and luteolin-7-glucoside as multi-targeted agents against Alzheimer's disease: a molecular docking study" . International Journal of Plant Based Pharmaceuticals 1 (2021 ): 56-64 <https://dergipark.org.tr/en/pub/ijpbp/issue/64282/976969>
Chicago İstifli, E. S. , Sarıkürkcü, C. "Assessment of apigenin-7-glucoside and luteolin-7-glucoside as multi-targeted agents against Alzheimer's disease: a molecular docking study". International Journal of Plant Based Pharmaceuticals 1 (2021 ): 56-64
RIS TY - JOUR T1 - Assessment of apigenin-7-glucoside and luteolin-7-glucoside as multi-targeted agents against Alzheimer's disease: a molecular docking study AU - Erman Salih İstifli , Cengiz Sarıkürkcü Y1 - 2021 PY - 2021 N1 - DO - T2 - International Journal of Plant Based Pharmaceuticals JF - Journal JO - JOR SP - 56 EP - 64 VL - 1 IS - 1 SN - -2791-7509 M3 - UR - Y2 - 2021 ER -
EndNote %0 International Journal of Plant Based Pharmaceuticals Assessment of apigenin-7-glucoside and luteolin-7-glucoside as multi-targeted agents against Alzheimer's disease: a molecular docking study %A Erman Salih İstifli , Cengiz Sarıkürkcü %T Assessment of apigenin-7-glucoside and luteolin-7-glucoside as multi-targeted agents against Alzheimer's disease: a molecular docking study %D 2021 %J International Journal of Plant Based Pharmaceuticals %P -2791-7509 %V 1 %N 1 %R %U
ISNAD İstifli, Erman Salih , Sarıkürkcü, Cengiz . "Assessment of apigenin-7-glucoside and luteolin-7-glucoside as multi-targeted agents against Alzheimer's disease: a molecular docking study". International Journal of Plant Based Pharmaceuticals 1 / 1 (December 2021): 56-64 .
AMA İstifli E. S. , Sarıkürkcü C. Assessment of apigenin-7-glucoside and luteolin-7-glucoside as multi-targeted agents against Alzheimer's disease: a molecular docking study. Int. J. Plant Bas. Pharm.. 2021; 1(1): 56-64.
Vancouver İstifli E. S. , Sarıkürkcü C. Assessment of apigenin-7-glucoside and luteolin-7-glucoside as multi-targeted agents against Alzheimer's disease: a molecular docking study. International Journal of Plant Based Pharmaceuticals. 2021; 1(1): 56-64.
IEEE E. S. İstifli and C. Sarıkürkcü , "Assessment of apigenin-7-glucoside and luteolin-7-glucoside as multi-targeted agents against Alzheimer's disease: a molecular docking study", International Journal of Plant Based Pharmaceuticals, vol. 1, no. 1, pp. 56-64, Dec. 2021

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