6-hydroxygeniposide, a potent -glucosidase inhibitor from Gardenia jasminoides growing in Viet Nam

Dinh Hoang Vu; Khac Hung Nguyen; Quang Duong Pham; Thi Viet Thanh Nguyen; Thi Phuong Anh Dinh; Van Tan Chu; Duc Tuan Cao; Hong Ngoc Tran; Gia Bao Truong; Dai Lam Tran

doi:10.15625/2525-2518/20030

Author affiliations

Authors

Vu Dinh Hoang Hanoi University of Science and Technology, 1 Dai Co Viet Street, Hanoi 10000, Viet Nam
Nguyen Khac Hung Hanoi University of Science and Technology, 1 Dai Co Viet Street, Hanoi 10000, Viet Nam https://orcid.org/0000-0001-5972-0131
Pham Quang Duong Institute for Tropical Technology, Vietnam Academy of Science and Technology, 18 Hoang Quoc Viet, Hanoi 10000, Vietnam
Nguyen Thi Viet Thanh Hanoi University of Science and Technology, 1 Dai Co Viet Street, Hanoi 10000, Viet Nam
Dinh Thi Phuong Anh Hanoi University of Science and Technology, 1 Dai Co Viet Street, Hanoi 10000, Viet Nam
Chu Van Tan Center for High Technology Research and Development, Vietnam Academy of Science and Technology, 18 Hoang Quoc Viet, Hanoi 10000, Vietnam
Cao Duc Tuan 4Hai Phong University of Medicine and Pharmacy, 72A Nguyen Binh Khiem Street, Haiphong, Viet Nam
Tran Hong Ngoc Faculty of Pharmacy, Phenikaa University, Yen Nghia, Ha Dong District, Hanoi 12116, Vietnam
Trương Gia Bao Gifted Class for Chemistry, High School for Gifted Students, Hanoi University of Science, Vietnam National University, Hanoi 10000, Vietnam
Tran Dai Lam Institute for Tropical Technology, Vietnam Academy of Science and Technology, 18 Hoang Quoc Viet, Hanoi 10000, Vietnam

DOI:

https://doi.org/10.15625/2525-2518/20030

Keywords:

6β-hydroxygeniposide, anti alpha-glucosidase, diabetes, Gardenia jasminoides, molecular docking, molecular dynamic simulation

Abstract

According to the statistics of WHO in 2019, diabetes was one of the top 10 causes of death in Vietnam and the incidence increasing day by day has required more effective treatment methods. For a long time, natural products have played an important role in drug screening programs. Gardenia jasminoides belongs to the Gardenia genus of Rubiaceae family, in which previous research showed potential ability in diabetes treatment through various mechanisms. In this study, 3 iridoids were isolated from G. jasminoides collected in Vietnam and the -glucosidase inhibitory was evaluated for the first time. The results showed 6-hydroxygeniposide (2) expressed the strongest activity with IC50 at 6.38 ± 0.12 M, meanwhile geniposide (1) and 6hydroxygeniposide (3) were inactive. The inhibitory mechanism of 6- hydroxygeniposide was revealed by molecular docking and molecular dynamics. 6- hydroxygeniposide competed and blocked p-nitrophenyl--D-glucopyranoside substrate reaching the reaction center of the enzyme, which was expressed through lower non-bonds interacting energy and stable binding affinity.

Downloads

Download data is not yet available.

References

Pham N. M., Eggleston K. - Diabetes prevalence and risk factors among Vietnamese adults: Findings from community-based screening programs. Diabetes Care 38 (5) (2015) e77–e78. doi.org/10.2337/dc14-3093

Tomic D., Shaw J., Magliano D. - The burden and risks of emerging complications of diabetes mellitus. Nat. Rev. Endocrinol. 18 (9) (2022) 525–539. doi.org/10.1038/s41574-022-00690-7

Tran T. D., Tu V. L., Hoang T. M., Dat T. V., Tam D. N. H., Phat N. H., Hung D. T., Huynh H. H, Do T. C., Le H. H., Minh L. H. N. - A review of the In Vitro inhibition of α-amylase and α-glucosidase by chalcone derivatives. Cureus 15 (4) (2023) e37267. doi.org/10.7759/cureus.37267

Brach A. R., Song H. - eFloras: New directions for online floras exemplified by the Flora of China Project. Taxon 55 (1) (2006) 188–192. doi.org/10.2307/25065540

Chen Y., Cheng Y., Tzeng C., Lee Y., Chang Y., Lee S., Tsai C., Chen J., Ceng Tzen J., Chang S. - Peroxisome proliferator-activated receptor activating hypoglycemic effect of Gardenia jasminoides Ellis aqueous extract and improvement of insulin sensitivity in steroid induced insulin resistant rats. BMC Complement Altern. Med. 14, 30 (2014). doi.org/10.1186/1472-6882-14-30

Wu S. S., Wang G., Liu Z., Rao J., Lv L., Xu W., Wu S. S., Zhang J., Lü L., Xu W., Wu S. S., Zhang J. - Effect of geniposide, a hypoglycemic glucoside, on hepatic regulating enzymes in diabetic mice induced by a high-fat diet and streptozotocin. Acta Pharmacol. Sin. 30 (2) (2009) 202–208. doi.org/10.1038/aps.2008.17

Wang G., Wu S., Xu W., Jin H., Zheng G., Li Z., Yuan X., Zhang J., Rao J., Wu S. -Geniposide inhibits high glucose-induced cell adhesion through the NF-kB signaling pathway in human umbilical vein endothelial cells. Acta Pharmacol. Sin. 31 (2010) 953–962. doi.org/10.1038/aps.2010.83

Hakamata W., Kurihara M., Okuda H., Nishio T., Oku T. - Design and screening strategies for alpha-glucosidase inhibitors based on enzymological information. Curr. Top. Med. Chem. 9 (1) (2009) 3–12. doi.org/10.2174/156802609787354306

Pathania S., Randhawa V., Bagler G. - Prospecting for novel plant-derived molecules of Rauvolfia serpentina as inhibitors of aldose reductase, a potent drug Target for diabetes and its complications. PLoS One 8 (4) (2013) e61327. doi.org/10.1371/journal.pone.0061327

Shivanika C., Deepak Kuma S., Venkataraghavan R., Pawan T., Sumitha A., Brindha Devi P. - Molecular docking, validation, dynamics simulations, and pharmacokinetic prediction of natural compounds against the SARS-CoV-2 main-protease. J. Biomol. Struct. Dyn. 40 (2) (2022) 585–611. doi.org/10.1080/07391102.2020.1815584.

Peytam F., Takalloobanafshi G., Saadattalab T., Norouzbahari M., Emamgholipour Z., Moghimi S., Firoozpour L., Bijanzadeh H., Faramarzi M., Mojtabavi S., Rashidi-Ranjbar P., Karima S., Pakraad R., Foroumadi A. - Design, synthesis, molecular docking, and in vitro α-glucosidase inhibitory activities of novel 3-amino-2,4-diarylbenzo[4,5]imidazo[1,2-a]pyrimidines against yeast and rat α-glucosidase. Sci. Rep. 11 (1) (2021), 11911. doi.org/10.1038/s41598-021-91473-z

Ali M., Malik K., Zaidi A., Farooq U., Bukhari S., Majeed Z., Mahnashi M., Nawazish S., Abdulwahab A., Alshaibari K. - In-vitro high-throughput library screening—Kinetics and molecular docking studies of potent inhibitors of α-glucosidase. PLoS One 18 (6) (2023) e0286159. doi.org/10.1371/journal.pone.0286159

Eberhardt J., Santos-Martins D., Tillack A., Forli S. - AutoDock Vina 1.2.0: New docking methods, expanded force field, and python bindings. J. Chem. Inf. Model. 61 (8) (2021) 3891–3898. doi.org/10.1021/acs.jcim.1c00203

Korb O., Stützle T., Exner T. - Proceedings of 5th International workshop on Ant Colony Optimization and Swarm Intelligence, Springer (2006) 247–258. doi.org/ 10.1007/11839088_22

Mysinger M., Carchia M., Irwin J., Shoichet B. - Directory of useful decoys, enhanced (DUD-E): Better ligands and decoys for better benchmarking. J. Med. Chem. 55 (14) (2012) 6582–6594. doi.org/10.1021/jm300687e

Hajian-Tilaki K. - Receiver Operating Characteristic (ROC) curve analysis for medical diagnostic test evaluation. Casp. J. Intern. Med. 4 (2) (2013) 627–635.

O’Boyle N., Banck M., James C., Morley C., Vandermeersch T., Hutchison G. - Open Babel: An open chemical toolbox. J. Cheminform. 3 (2011) 33. doi.org/10.1186/1758-2946-3-33

Abraham M., Murtola T., Schulz R., Páll S., Smith J., Hess B., Lindahl E. - GROMACS: High performance molecular simulations through multi-level parallelism from laptops to supercomputers. SoftwareX 1–2 (2015) 19–25. doi.org/ 10.1016/j.softx.2015.06.001

Lemkul J. - From proteins to perturbed hamiltonians: A Suite of tutorials for the GROMACS-2018 molecular simulation package. Living J. Comput. Mol. Sci. 1(1) (2019) 1–53. doi.org/10.33011/livecoms.1.1.5068

Laskowski R., Swindells M. - LigPlot+: multiple ligand-protein interaction diagrams for drug discovery. J. Chem. Inf. Model. 51 (10) (2011) 2778–2786. doi.org/ 10.1021/ci200227u

Morota T., Sasaki H., Nishimura H., Sugama K., Chin M., Mitsuhashi H. - Two iridoid glycosides from Rehmannia glutinosa. Phytochemistry 28 (8) (1989) 2149–2153. doi.org/10.1016/S0031-9422(00)97934-2

Çalış İ., Weas A., Soliman Yusufoğlu H., Dönmez A., Jensen S. - Iridoid glucosides from Wendlandia ligustroides (Boiss. &Hohen.) Blakelock. Saudi Pharm. J. 28 (7) (2020) 814–818. doi.org/10.1016/j.jsps.2020.05.009

Velázquez-Fiz M., Díaz-Lanza A., Fernández-Matellano L. - Iridoids from Plantago Lagopus. Pharm. Biol. 38 (4) (2000) 268–270. doi.org/10.1076/1388-0209(200009)3841-AFT268

Hernández-Rodríguez M., Rosales-Hernández M. C., Mendieta-Wejebe J. E., Martínez-Archundia M., Correa Basurto J. - Current tools and methods in molecular dynamics (MD) simulations for drug design. Curr. Med. Chem. 23 (34) (2016) 3909–3924. doi.org/ 10.2174/0929867323666160530144742.

Hevener K., Zhao W., Ball D., Babaoglu K., Qi J., White S., Lee R.- Validation of molecular docking programs for virtual screening against dihydropteroate synthase. J. Chem. Inf. Model. 49 (2) (2009) 444–460. doi.org/10.1021/ci800293n.

Isomaltase (alpha-1,6-glucosidase) from Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast). https://www.uniprot.org/uniprotkb/P53051/entry (accessed 20 July 2022). .

Tang H., Zhao D., Xue Z. - Exploring the interaction between Salvia miltiorrhiza and α-glucosidase: insights from computational analysis and experimental studies. RSC Adv. 8 (44) (2018) 24701–24710. doi.org/10.1039/C8RA04772C

Oyewusi H., Wu Y., Safi S., Wahab R., Hatta M., Batumalaie K. - Molecular dynamics simulations reveal the inhibitory mechanism of Withanolide A against α-glucosidase and α-amylase. J. Biomol. Struct. Dyn. 41 (13) 6203–6218. doi.org/10.1080/ 07391102.2022.2104375

Wang X., Deng Y., Zhang Y., Zhang C., Liu L., Liu Y., Jiang J., Xie P., Huang L.- Screening and evaluation of novel α-glucosidase inhibitory peptides from Ginkgo biloba seed cake based on molecular docking combined with molecular dynamics simulation. J. Agric. Food Chem. 71 (27) (2023) 10326–10337. doi.org/10.1021/acs.jafc.3c00826