Abstract
Alzheimer’s disease is one of the most common causes of dementia. Acetylcholinesterase has been considered as the main therapeutic target in the treatment of Alzheimer’s disease. Natural products are the richest source of lead compounds for the discovery and development of new drugs. In the present contribution, the hierarchical biology–oriented method was applied to discover the active gradients of F. pseudalliacea root as AChE inhibitors. The Kamonolol acetate was extracted and identified from the n-hexane extract of F. pseudalliacea root. The Kamonolol acetate inhibited the AChE with IC50: 63.9 μM. Molecular modeling studies showed that Kamonolol acetate interacted with CAS and PAS of AChE active site. Kinetics in accompany with molecular modeling studies demonstrated that Kamonolol acetate inhibited AChE in the mixed-type model. The results indicated that Kamonolol acetate could be considered as a valuable lead compound in the design of AChE inhibitors.
Similar content being viewed by others
References
Goedert M, Spillantini MG (2006) A century of Alzheimer's disease. Science 314(5800):777–781
Qiu C, Kivipelto M, von Strauss E (2009) Epidemiology of Alzheimer's disease: occurrence, determinants, and strategies toward intervention. Dialogues Clin Neurosci 11(2):111
Francis PT, Palmer AM, Snape M, Wilcock GK (1999) The cholinergic hypothesis of Alzheimer’s disease: a review of progress. J Neurol Neurosurg Psychiatry 66(2):137–147
Bush AI (2001) Therapeutic targets in the biology of Alzheimer's disease. Curr Opin Psychiatry 14(4):341–348
Birks JS (2006) Cholinesterase inhibitors for Alzheimer's disease. Cochrane Database Syst Rev 1
Newman DJ, Cragg GM, Holbeck S, Sausville EA (2002) Natural products and derivatives as leads to cell cycle pathway targets in cancer chemotherapy. Curr Cancer Drug Targets 2(4):279–308
Williams DH, Stone MJ, Hauck PR, Rahman SK (1989) Why are secondary metabolites (natural products) biosynthesized? J Nat Prod 52(6):1189–1208
Houghton PJ, Ren Y, Howes M-J (2006) Acetylcholinesterase inhibitors from plants and fungi. Nat Prod Rep 23(2):181–199
Mukherjee PK, Kumar V, Mal M, Houghton PJ (2007) Acetylcholinesterase inhibitors from plants. Phytomedicine 14(4):289–300
de Souza LG, Rennó MN, Figueroa-Villar JD (2016) Coumarins as cholinesterase inhibitors: a review. Chem Biol Interact 254:11–23
Kasaian J, Iranshahy M, Iranshahi M (2014) Synthesis, biosynthesis and biological activities of galbanic acid–a review. Pharm Biol 52(4):524–531
Salem SB, Jabrane A, Harzallah-Skhiri F, Jannet HB (2013) New bioactive dihydrofuranocoumarins from the roots of the Tunisian Ferula lutea (Poir.) Maire. Bioorg Med Chem Lett 23(14):4248–4252
Dincel D, HATIPOĞLU SD, GÖREN AC, TOPÇU G (2013) Anticholinesterase furocoumarins from Heracleum platytaenium, a species endemic to the Ida Mountains. Turk J Chem 37(4):675–683
Awang K, Chan G, Litaudon M, Ismail NH, Martin M-T, Gueritte F (2010) 4-Phenylcoumarins from Mesua elegans with acetylcholinesterase inhibitory activity. Biorg Med Chem 18(22):7873–7877
Pimenov M, Leonov M (2004) The Asian Umbelliferae biodiversity database (ASIUM) with particular reference to South-West Asian taxa. Turk J Bot 28(1–2):139–145
Ghareeb DA, ElAhwany AM, El-mallawany SM, Saif AA (2014) In vitro screening for anti-acetylcholiesterase, anti-oxidant, anti-glucosidase, anti-inflammatory and anti-bacterial effect of three traditional medicinal plants. Biotechnol Biotechnol Equip 28(6):1155–1164
Dehpour AA, Ebrahimzadeh MA, Fazel NS, Mohammad NS (2009) Antioxidant activity of the methanol extract of Ferula assafoetida and its essential oil composition. Grasas Aceites 60(4):405–412
Lee C-L, Chiang L-C, Cheng L-H, Liaw C-C, Abd El-Razek MH, Chang F-R, Wu Y-C (2009) Influenza A (H1N1) antiviral and cytotoxic agents from Ferula assa-foetida. J Nat Prod 72(9):1568–1572
Fatehi M, Farifteh F, Fatehi-Hassanabad Z (2004) Antispasmodic and hypotensive effects of Ferula asafoetida gum extract. J Ethnopharmacol 91(2–3):321–324
Abu-Zaiton AS (2010) Anti-diabetic activity of Ferula assafoetida extract in normal and alloxan-induced diabetic rats. Pak J Biol Sci 13(2):97
Vijayalakshmi SA, Bhat P, Chaturvedi A, Bairy K, Kamath S (2012) Evaluation of the effect of Ferula asafoetida Linn. gum extract on learning and memory in Wistar rats. Indian J Pharm 44(1):82
Adhami H-R, Fitz V, Lubich A, Kaehlig H, Zehl M, Krenn L (2014) Acetylcholinesterase inhibitors from galbanum, the oleo gum-resin of Ferula gummosa Boiss. Phytochem Lett 10:lxxxii–lxxxvii
Xing Y, Li N, Zhou D, Chen G, Jiao K, Wang W, Si Y, Hou Y (2017) Sesquiterpene coumarins from Ferula sinkiangensis act as neuroinflammation inhibitors. Planta Med 83(01/02):135–142
Dastan D, Salehi P, Gohari AR, Zimmermann S, Kaiser M, Hamburger M, Khavasi HR, Ebrahimi SN (2012) Disesquiterpene and sesquiterpene coumarins from Ferula pseudalliacea, and determination of their absolute configurations. Phytochemistry 78:170–178
Dastan D, Salehi P, Gohari AR, Ebrahimi SN, Aliahmadi A, Hamburger M (2014) Bioactive sesquiterpene coumarins from Ferula pseudalliacea. Planta Med 80(13):1118–1123
Suttie J (1987) The biochemical basis of warfarin therapy. The new dimensions of warfarin prophylaxis. Springer, Berlin, pp 3–16
Ferreira SZ, Carneiro HC, Lara HA, Alves RB, Resende JM, Oliveira HM, Silva LM, Santos DA, Freitas RP (2015) Synthesis of a new peptide–coumarin conjugate: a potential agent against cryptococcosis. ACS Med Chem Lett 6(3):271–275
Neyts J, Clercq ED, Singha R, Chang YH, Das AR, Chakraborty SK, Hong SC, Tsay S-C, Hsu M-H, Hwu JR (2009) Structure−activity relationship of new anti-hepatitis C virus agents: heterobicycle−coumarin conjugates. J Med Chem 52(5):1486–1490
Khan KM, Saify ZS, Khan MZ, Zia-Ullah CMI, Atta-ur-Rahman PS, Chohan ZH, Supuran CT (2004) Synthesis of coumarin derivatives with cytotoxic, antibacterial and antifungal activity. J Enzyme Inhib Med Chem 19(4):373–379
Sashidhara KV, Kumar A, Kumar M, Sarkar J, Sinha S (2010) Synthesis and in vitro evaluation of novel coumarin–chalcone hybrids as potential anticancer agents. Bioorg Med Chem Lett 20(24):7205–7211
Kontogiorgis C, Nicolotti O, Mangiatordi GF, Tognolini M, Karalaki F, Giorgio C, Patsilinakos A, Carotti A, Hadjipavlou-Litina D, Barocelli E (2015) Studies on the antiplatelet and antithrombotic profile of anti-inflammatory coumarin derivatives. J Enzyme Inhib Med Chem 30(6):925–933
Kurt BZ, Gazioglu I, Sonmez F, Kucukislamoglu M (2015) Synthesis, antioxidant and anticholinesterase activities of novel coumarylthiazole derivatives. Bioorg Chem 59:80–90
Ellman GL, Courtney KD, Andres Jr V, Featherstone RM (1961) A new and rapid colorimetric determination of acetylcholinesterase activity. Biochem Pharmacol 7(2):88–95
Morris GM, Huey R, Lindstrom W, Sanner MF, Belew RK, Goodsell DS, Olson AJ (2009) AutoDock4 and AutoDockTools4: automated docking with selective receptor flexibility. J Comput Chem 30(16):2785–2791
Razzaghi-Asl N, Ebadi A, Edraki N, Shahabipour S, Miri R (2013) Fragment-based binding efficiency indices in bioactive molecular design: a computational approach to BACE-1 inhibitors. Iran J Pharm Res 12(3):423
Ebadi A, Razzaghi-Asl N, Shahabipour S, Miri R (2014) Ab-initio and conformational analysis of a potent VEGFR-2 inhibitor: a case study on Motesanib. Iran J Pharm Res 13(2):405
Razzaghi-Asl N, Sepehri S, Ebadi A, Miri R, Shahabipour S (2015) Molecular docking and quantum mechanical studies on biflavonoid structures as BACE-1 inhibitors. Struct Chem 26(2):607–621
Van Der Spoel D, Lindahl E, Hess B, Groenhof G, Mark AE, Berendsen HJ (2005) GROMACS: fast, flexible, and free. J Comput Chem 26(16):1701–1718
Schüttelkopf AW, Van Aalten DM (2004) PRODRG: a tool for high-throughput crystallography of protein–ligand complexes. Acta Crystallogr Sect D Biol Crystallogr 60(8):1355–1363
Jakalian A, Jack DB, Bayly CI (2002) Fast, efficient generation of high-quality atomic charges. AM1-BCC model: II. Parameterization and validation. J Comput Chem 23(16):1623–1641
Hess B, Bekker H, Berendsen HJ, Fraaije JG (1997) LINCS: a linear constraint solver for molecular simulations. J Comput Chem 18(12):1463–1472
Darden T, York D, Pedersen L (1993) Particle mesh Ewald: an N·log (N) method for Ewald sums in large systems. J Chem Phys 98(12):10089–10092
Pohanka M, Hrabinova M, Kuca K, Simonato J-P (2011) Assessment of acetylcholinesterase activity using indoxylacetate and comparison with the standard Ellman’s method. Int J Mol Sci 12(4):2631–2640
Shi J, Tu W, Luo M, Huang C (2017) Molecular docking and molecular dynamics simulation approaches for identifying new lead compounds as potential AChE inhibitors. Mol Simul 43(2):102–109
Kiametis AS, Silva MA, Romeiro LA, Martins JB, Gargano R (2017) Potential acetylcholinesterase inhibitors: molecular docking, molecular dynamics, and in silico prediction. J Mol Model 23(2):67
Koehn FE, Carter GT (2005) The evolving role of natural products in drug discovery. Nat Rev Drug Discov 4(3):206
Funding
The study was funded by the Vice-chancellor for Research and Technology, Hamadan University of Medical Sciences (No. 950117130).
Author information
Authors and Affiliations
Corresponding author
Ethics declarations
Conflict of interest
The authors declare that they have no conflict of interests.
Additional information
Publisher’s note
Springer Nature remains neutral with regard to jurisdictional claims in published maps and institutional affiliations.
Rights and permissions
About this article
Cite this article
Dastan, D., Validi, S. & Ebadi, A. Kamonolol acetate from Ferula pseudalliacea as AChE inhibitor: in vitro and in silico studies. Struct Chem 31, 965–973 (2020). https://doi.org/10.1007/s11224-019-01473-z
Received:
Accepted:
Published:
Issue Date:
DOI: https://doi.org/10.1007/s11224-019-01473-z