Studies to understand the effect of Centella asiatica on A-beta (42) aggregation in vitro

Order of Publishing in Issue: 
10
Volume :4
Issue :2
April, 2010 - June, 2010
Page No: 
716-724
Authors: 
Ramesh, B.N [1] , Indi, S.S [2] , Rao, K.S.J. [1]*
Address: 
[1] Department of Biochemistry and Nutrition, Central Food Technological Research Institute, CSIR Unit, Mysore-570020, India
Address: 
[2] Department of Microbiology and Cell Biology, Indian Institute of Science, Bangalore, India.
Email-ID: 
kjr5n2009@gmail.com

Abstract: Amyloid beta  is the major pathological and etiological factor implicated in Alzheimer’s disease (AD). Amyloid beta (42) inherently self assembles toform oligomers and fibrils through multifactorial aggregation process. The oligomers and fibrils have toxic effects and may lead to neuronal dysfunction.The inhibition of formation of oligomers and fibrils is a novel strategy in drug development programs for AD. There are limited studiesto show to that Centella asiatica has a memory enhancing, anti-acetlylcholinesterase and antioxidant properties. But there are no studies to insightwhether C. asiatica prevents Amyloid beta fibrils formation from monomers and oligomers and also to understand whether C. asiatica destabilize thepreformed fibrils. Our present study focused on, i) whether the C. asiatica leaf aqueous extract prevent the formation of oligomers and aggregatesfrom monomer? (Phase I: Amyloid beta (42) + extract co –incubation), ii) Whether the C. asiatica aqueous extract prevent the formation of fibrilsfrom oligomers (Phase II- extract added after oligomers formation) and iii) whether the aqueous extract dis-aggregates the pre-formed fibrils(Phase III - aqueous extract added to matured fibrils and incubated for 8 days). The aggregation kinetics was studied using thioflavin-T assayand Transmission Electron Microscopy (TEM). The results showed that C. asiatica aqueous extract could not able to inhibit the A? aggregationboth from monomer and oligomers and also could not able to dis-integrate the preformed fibrils. These intriguing results are discussed.

Keywords: 
Aβ(42), Fibrils, Aggregation, Thioflavin-T, Transmission Electron Microscopy, Centella asiatica
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