In silico studies were performed to understand the binding mechanism of these compounds to aldose reductase
📌 3 Maddede Bu Makale
🎯
Amaç & Hipotez:Phytochemical investigation of the aerial parts of Eryngium caeruleum led to the isolation of two new source flavone glycosides (1 and 2).
📊
Temel Bulgular & Veri:The structures of these compounds were determined with the help of one- and two-dimensional (1D- and 2D-) NMR techniques including 1H-NMR, 13C-NMR, HMQC, HMBC, 1H-1H COSY, and NOESY experiments.
💡
Sonuç & Katkı:In silico studies were performed to understand the binding mechanism of these compounds to aldose reductase
🔬Tür:Araştırma Makalesi
📍Kapsam:Genişletilmiş Akademik Örneklem
⚙️Değişkenler:Alan Parametreleri
Abstract
Phytochemical investigation of the aerial parts of Eryngium caeruleum led to the isolation of two new source flavone glycosides (1 and 2). The structures of these compounds were determined with the help of one- and two-dimensional (1D- and 2D-) NMR techniques including 1H-NMR, 13C-NMR, HMQC, HMBC, 1H-1H COSY, and NOESY experiments. The compounds were studied for their in vitro aldose reductase (ALR1 and ALR2) and glucosidase (α and β) inhibitory activities, and antiglycation potential. Both the compounds showed higher inhibition potential against ALR1 than ALR2. Compound 2 showed three fold higher potency against ALR2 than the reference drug Sorbinil. In silico studies were performed to understand the binding mechanism of these compounds to aldose reductase
🔖
Bu Makaleye Atıf Yap
AHMAD, V. U., REHMAN, A. U., HASHMİ, M. A., TEHSEEN, Y., KHAN, A., KHAN, S. S., IQBAL, J., IQBAL, J., KHAN, S., FAROOQ, U. (2017). Antidiabetic Flavonol Glycosides from Eryngium caeruleum. Records of Natural Products, Cilt: 11 - Sayı: 2, 229–258. https://ajindex.com/articles/308349
E. A. Irondi, G. Oboh, A. A. Akindahunsi, A. A. Boligon, and M. L. Athayde (2014). Phenolic composition and inhibitory activity of Mangifera indica and Mucuna urens seeds extracts against key enzymes linked to the pathology and complications of type 2 diabetes, Asian Pac. J. Trop. Biomed. 4, 903-910
D. G. Lee, K. H. Lee, K.-W. Park, C. K. Han, B.-Y. Ryu, E. J. Cho, and S. Lee (2015). Isolation and Identification of Flavonoids with Aldose Reductase Inhibitory Activity from Petasites japonicus, Asian J. Chem. 27, 991
C.-L. Zhang, Y. Wang, Y.-F. Liu, D. Liang, Z.-Y. Hao, H. Luo, R.-Y. Chen, Z.-Y. Cao, and D.-Q. Yu (2016). Two new flavonoid glycosides from Iris tectorum, Phytochem. Lett. 15, 63-65
S. Narayanan (1993). Aldose reductase and its inhibition in the control of diabetic complications, Ann. Clin. Lab. Sci. 23, 148-158
P. F. Kador, Y. Akagi, and J. H. Kinoshita (1986). The effect of aldose reductase and its inhibition on sugar cataract formation, Metabolis. 35, 15-19
R. Van Heyningen (1959). Formation of polyols by the lens of the rat with ‘Sugar’ cataract, Nature 184, 194-195
M. J. Peterson, R. Sarges, C. E. Aldinger, and D. P. MacDonald (1979). CP-45,634: a novel aldose reductase inhibitor that inhibits polyol pathway activity in diabetic and galactosemic rats, Metabolis. 28, 456-461
V. F. Carvalho, E. O. Barreto, M. F. Serra, R. S. B. Cordeiro, M. A. Martins, Z. B. Fortes, and P. M. R. e Silva (2006). Aldose reductase inhibitor zopolrestat restores allergic hyporesponsiveness in alloxandiabetic rats, Eur. J. Pharmacol. 549, 173-178
S. R. Thorpe and J. W. Baynes (2003). Maillard reaction products in tissue proteins: new products and new perspectives, Amino Acids 25, 275-281
R. G. Khalifah, J. W. Baynes, and B. G. Hudson (1999). Amadorins: novel post-Amadori inhibitors of advanced glycation reactions, Biochem. Biophys. Res. Commun. 257, 251-258
T. Yu, J. L. Robotham, and Y. Yoon (2006). Increased production of reactive oxygen species in hyperglycemic conditions requires dynamic change of mitochondrial morphology, Proc. Natl. Acad. Sci. USA 103, 2653-2658
M. Brownlee (1994). Lilly Lecture 1993. Glycation and diabetic complications, Diabetes 43, 836-841
M. Peppa, J. Uribarri, and H. Vlassara (2004). The role of advanced glycation end products in the development of atherosclerosis, Curr. Diabetes Rep. 4, 31-36.[14] J. Chen, Y. Wu, J. Zou, and K. Gao (2016). α-Glucosidase inhibition and