Skip to content
2000
Volume 22, Issue 11
  • ISSN: 1570-1786
  • E-ISSN: 1875-6255

Abstract

Steroidal saponins are natural compounds known to have anticancer activity by inducing apoptosis through inhibition of Bcl-2. This study was carried out on the potency, mechanism, and binding affinity of steroidal saponins present from var. as Bcl-2 inhibitor of colorectal cancer using molecular docking and molecular dynamics simulation. All steroidal saponins exhibited hydrogen bonds in molecular docking, Van der Waals, and hydrophobic interactions. The binding potentials of steroidal saponins collected in previous studies and a reference compound, navitoclax, as target protein 6GL8 of BCL-2 inhibitor of colorectal cancer, were examined using molecular docking. The results showed the binding stabilities as -8.28, -8.87, -9.29, -11.09, -11.16, and -8.34 kcal/mol, respectively. Given the limited in-silico studies on pregnane saponins, we considered the extensive interest in these compounds. So, molecular dynamics studies were carried out to better comprehend the dynamics of ligands within the binding pocket of the target protein. Molecular dynamics simulation revealed that the binding of parasiticoside B to the 6GL8 receptor was stable and strong, based on their RMSD, RMSF, and the number of hydrogen bonds throughout the simulation. From the molecular interaction analysis derived from molecular dynamic trajectories of each ligand-bound complex, these interacting amino acids might be determined to play a crucial role in binding with the ligands of the 6GL8 active site. Parasiticoside B could be a good candidate for new inhibitors of anti-apoptotic BCL-2 proteins in colorectal cancer.

© 2025 Bentham Science Publishers
Loading

Article metrics loading...

/content/journals/loc/10.2174/0115701786363779250528013022
2025-11-01
2025-12-22

  • From This Site

    /content/journals/loc/10.2174/0115701786363779250528013022
    dcterms_title,dcterms_subject,pub_keyword
    -contentType:Contributor -contentType:Concept -contentType:Institution
    10
    5
Loading full text...

Full text loading...

References

  1. BrownJ.S. AmendS.R. AustinR.H. GatenbyR.A. HammarlundE.U. PientaK.J. Mol. Cancer Res.202321111142114710.1158/1541‑7786.MCR‑23‑0411 37409952
     [Google Scholar]
  2. WongR.S.Y. J. Exp. Clin. Cancer Res.20113018710.1186/1756‑9966‑30‑87 21943236
     [Google Scholar]
  3. HungR.W.Y. ChowA.W. Can. J. Infect. Dis.199782103109 22514484
     [Google Scholar]
  4. ElmoreS. Toxicol. Pathol.200735449551610.1080/01926230701320337 17562483
     [Google Scholar]
  5. CzabotarP.E. LesseneG. StrasserA. AdamsJ.M. Nat. Rev. Mol. Cell Biol.2014151496310.1038/nrm3722 24355989
     [Google Scholar]
  6. QianS. WeiZ. YangW. HuangJ. YangY. WangJ. Front. Oncol.20221298536310.3389/fonc.2022.985363 36313628
     [Google Scholar]
  7. KruakaewS. SinghaS. SeekaC. MongkolvisutW. SutthivaiyakitS. Phytochem. Lett.20182711912210.1016/j.phytol.2018.07.014
     [Google Scholar]
  8. Ab-RahimN. IsmailW.I. Fikri RoslanM.N. Hafiz MailM. Che LaminR.A. IsmailS. Biomed. Pharmacol. J.201912285786210.13005/bpj/1710
     [Google Scholar]
  9. SrivastavaR. NarainD. DeepakD. KhareA. Nat. Prod Commun20072111934578X070020110710.1177/1934578X0700201107
     [Google Scholar]
  10. RezaM.S.H. MandalC. AlamK.A. SalamA. RahmanM.A. AminM.R. HudaM.N. GhostN.C. AliM.R. AhmedF. J. Pharmacol. Toxicol.20072875375610.3923/jpt.2007.753.756
     [Google Scholar]
  11. SpargS.G. LightM.E. van StadenJ. J. Ethnopharmacol.2004942-321924310.1016/j.jep.2004.05.016 15325725
     [Google Scholar]
  12. BouabdallahS. Al-MaktoumA. AminA. Cancers20231515390010.3390/cancers15153900 37568716
     [Google Scholar]
  13. HoangC.V. TuT.Q. NguyenL.T.N. NguyenH.D. NguyenQ.H. ChuM.H. Rec. Nat. Prod.202317610461051
     [Google Scholar]
  14. TuT.Q. NguyenY.T.H. Thi Ngoc NguyenL. Duc NguyenH. ChuM.H. Nat. Prod. Res.202539226927410.1080/14786419.2023.2261601 37737149
     [Google Scholar]
  15. Bitencourt-FerreiraG. Veit-AcostaM. De AzevedoW.F. In: Docking Screens for Drug Discovery.New YorkHumana2019799110.1007/978‑1‑4939‑9752‑7_6
     [Google Scholar]
  16. RighettiP.G. BoschettiE. In: Low-Abundance Proteome Discovery.AmsterdamElsevier Science B. V20137915710.1016/B978‑0‑12‑401734‑4.00004‑X
     [Google Scholar]
  17. LippertT. RareyM. J. Cheminform.2009111310.1186/1758‑2946‑1‑13 20298519
     [Google Scholar]
  18. TerefeE.M. GhoshA. Bioinform. Biol. Insights2022161177932222112560510.1177/11779322221125605 36185760
     [Google Scholar]
  19. VaghasiyaM.D. MendaparaJ.V. VaghasiyaS.P. RajaniD.P. AhmadI. PatelH. KumariP. J. Mol. Struct.2023129413630810.1016/j.molstruc.2023.136308
     [Google Scholar]
  20. LiJ. ShenJ. LiX. QinZ. JiangZ. SunS. LiZ. J. Indian Chem. Soc.20241011210147810.1016/j.jics.2024.101478
     [Google Scholar]
  21. PhongN.V. HeoM.S. VinhL.B. KimY.H. YangS.Y. J. Mol. Struct.2024131713913510.1016/j.molstruc.2024.139135
     [Google Scholar]
  22. AldakheelF.M. Arch. Biochem. Biophys.202476111015710.1016/j.abb.2024.110157 39307263
     [Google Scholar]
  23. LiuY. TongJ.B. FanX. Process. Biochem.202414627328610.1016/j.procbio.2024.07.036
     [Google Scholar]
  24. MaitiR. Van DomselaarG.H. ZhangH. WishartD.S. Nucleic Acids Res.200432Web ServerW590W59410.1093/nar/gkh47715215457
     [Google Scholar]
  25. HanwellM.D. CurtisD.E. LonieD.C. VandermeerschT. ZurekE. HutchisonG.R. J. Cheminform.2012411710.1186/1758‑2946‑4‑17 22889332
     [Google Scholar]
  26. Van Der SpoelD. LindahlE. HessB. GroenhofG. MarkA.E. BerendsenH.J.C. J. Comput. Chem.200526161701171810.1002/jcc.20291 16211538
     [Google Scholar]
  27. GuexN. PeitschM.C. Electrophoresis199718152714272310.1002/elps.1150181505 9504803
     [Google Scholar]
  28. ZoeteV. CuendetM.A. GrosdidierA. MichielinO. J. Comput. Chem.201132112359236810.1002/jcc.21816 21541964
     [Google Scholar]
  29. PettersenE.F. GoddardT.D. HuangC.C. CouchG.S. GreenblattD.M. MengE.C. FerrinT.E. J. Comput. Chem.200425131605161210.1002/jcc.20084 15264254
     [Google Scholar]
/content/journals/loc/10.2174/0115701786363779250528013022
Loading
In silico Studies of Saponins from Hoya Verticillata var. Verticillate with Important Apoptosis Potency
Lett. Org. Chem. 22, 846 (2025); https://doi.org/10.2174/0115701786363779250528013022
/content/journals/loc/10.2174/0115701786363779250528013022
/content/journals/loc/10.2174/0115701786363779250528013022
Loading

Data & Media loading...


  • Article Type:     Research Article
Keyword(s): Colorectal cancer; Hoya parasitica; Hoya verticillata var. verticillata; molecular docking; molecular dynamic simulation; steroidal saponin

Most Cited Most Cited RSS feed

This is a required field
Please enter a valid email address
Approval was a Success
Invalid data
An Error Occurred
Approval was partially successful, following selected items could not be processed due to error
Please enter a valid_number test