Catechins and procyanidins of ginkgo biloba show potent activities towards the inhibition of β-amyloid peptide aggregation and destabilization of preformed fibrils

Molecules

Volumn 19, Issue 4, 2014, Pages 5119-5134

  Xie, Haiyan ^a   Wang, Jing Rong ^a,b   Yau, Lee Fong ^a,b   Liu, Yong ^a   Liu, Liang ^a,b   Han, Quan Bin ^a   Zhao, Zhongzhen ^a   Jiang, Zhi Hong ^a,b  

^a HONG KONG BAPTIST UNIVERSITY   (Hong Kong)

^b China jack1987168 163com   (Macao)

Author keywords

Catechin; Ginkgo biloba; Inhibition of aggregation; Procyanidin; amyloid

Indexed keywords

AMYLOID BETA PROTEIN; AMYLOID BETA-PROTEIN (1-42); BENZOPYRAN DERIVATIVE; BIFLAVONOID; CATECHIN; GALLOCATECHIN; GINKGO BILOBA EXTRACT 761; PEPTIDE FRAGMENT; PLANT EXTRACT; PROANTHOCYANIDIN; PROCYANIDIN B1; PROCYANIDIN B3;

ANALOGS AND DERIVATIVES; ANTAGONISTS AND INHIBITORS; CHEMISTRY; GINKGO BILOBA; HUMAN; ISOLATION AND PURIFICATION; PLANT LEAF; STRUCTURE ACTIVITY RELATION;

AMYLOID BETA-PEPTIDES; BENZOPYRANS; BIFLAVONOIDS; CATECHIN; GINKGO BILOBA; HUMANS; PEPTIDE FRAGMENTS; PLANT EXTRACTS; PLANT LEAVES; PROANTHOCYANIDINS; STRUCTURE-ACTIVITY RELATIONSHIP;

EID: 84899523235     PISSN: None     EISSN: 14203049     Source Type: Journal    
DOI: 10.3390/molecules19045119     Document Type: Article

References (12)

1. De Felice, F.G.; Houzel, J.C.; Garcia-Abreu, J.; Louzada, P.R.F.; Afonso, R.C.; Meirelles, M.N.L.; Lent, R.; Neto, V.M.; Frerreira, S.T. Inhibition of Alzheimer's disease ß-amyloid aggregation, neurotoxicity, and in vivo deposition by nitrophenols: Implications for Alzheimer's therapy. FASEB J. 2001, doi:10.1096/00-0676fje.
2. Xie, H.-Y.; Wang, J.-R.; Yau, L.-F.; Liu, Y.; Liu, L.; Han, Q.-B.; Zhao, Z.-Z.; Jiang, Z.-H. Quantitative analysis of the flavonoid glycosides and terpene trilactones in the extract of Ginkgo biloba and evaluation of their inhibitory activity towards fibril formation of ß-amyloid peptide. Molecules 2014, 19, 4466-4478.
3. Van Beek, T.A.; Montorob, P. Chemical analysis and quality control of Ginkgo biloba leaves, extracts and phytopharmaceuticals. J. Chromatogr. A 2009, 1216, 2002-2032.
4. Ono, K.; Hasegawa, K.; Yamada, K.; Naiki, H. Nicotine breaks down performed Alzheimer's beta-amyloid fibrils in vitro. Biol. Psychiat. 2002, 52, 880-886.
5. Porat, Y.; Abramowitz, A.; Gazit, E. Inhibition of amyloid fibril formation by polyphenols: Structural similarity and aromatic interactions as a common inhibition mechanism. Chem. Biol. Drug. Des. 2006, 67, 27-37.
6. Mizukami, Y.; Sawai, Y.; Yamaguchi, Y. Simultaneous analysis of catechins, gallic acid, strictinin, and purine alkaloids in green tea by using catechol as an internal standard. J. Agric. Food Chem. 2007, 55, 4957-4964.
7. Zhang, H.Y.; Wang, J.R.; Yau, L.F.; Ho, H.M.; Chan, C.L.; Hu, P.; Liu, L.; Jiang, Z.H. A cellular lipidomic study on the Aß-induced neurotoxicity and neuroprotective effects of EGCG by using UPLC/MS-based glycerolipids profiling and multivariate analysis. Mol. Biosyst. 2012, 8, 3208-3215.
8. Bai, L.P.; Ho, H.M.; Ma, D.L.; Yang, H.; Fu, W.C.; Jiang, Z.H. Aminoglycosylation can enhance the G-quadruplex binding activity of epigallocatechin. PLoS One 2013, 8, e53962.
9. Rezai-Zadeh, K.; Shytle, D.; Sun, N.; Mori, T.; Hou, H.Y.; Jeanniton, D.; Ehrhart, J.; Townsend, K.; Zeng, J.; Morgan, D.; et al. Green tea epigallocatechin-3-gallate (EGCG) modulates amyloid precureor protein cleavage and reduces cerebral amyloidosis in Alzheimer transgenic mice. J. Neurosci. 2005, 25, 8807-8814.
10. Haque, A.M.; Hashimoto M.; Katakura, M.; Hara, Y.; Shido, O. Green tea catechins prevent cognitive deficits caused by Aß1-40 in rats. J. Nutr. Biochem. 2008, 19, 619-626.
11. Rezai-Zadeh K.; Arendash G.W.; Hou H.Y.; Fernandez, F.; Jensen, M.; Runfeldt, M.; Shytle, R.D.; Tan, J. Green tea epigallocatechin-3-gallate (EGCG) reduces ß-amyloid mediated cognitive impairment and modulates tau pathology in Alzheimer transgenic mice. Brain Res. 2008, 1214, 177-187.
12. Nie, Q.; Du, X.G.; Geng, M.Y. Small molecule inhibitors of amyloid ßpeptide aggregation as a potential therapeutic strategy for Alzheimer's disease. Acta Pharm. Sin. 2011, 32, 545-551.