Document Detail

A novel in vitro filter trap assay identifies tannic acid as an amyloid aggregation inducer for HET-s.
MedLine Citation:
PMID:  16621084     Owner:  NLM     Status:  MEDLINE    
In this work we present an easy and low cost in vitro filter trap assay to quickly identify direct actors on amyloid prion aggregation. We chose the recombinant purified prion protein HET-s from Podospora anserina as a reference. HET-s was labelled with a fluorophore prior to aggregation assays in a 96 well micro-array system. Aggregation assays were carried out in presence of a number of chemical compounds, followed by a filter trap assay through a cellulose acetate membrane and the straight detection of retained fluorescent amyloid fibres. We tested 22 chemical compounds from which 11 have already been described to affect various prions and other amyloid proteins. Four compounds showed direct effects on the aggregation of HET-s. ZnCl seemed to prevent the formation of amyloid fibres. Puzzlingly, three members of the group of tannins (tannic acid, epigallocatechin and epigallocatechin-gallate) had accelerant properties on amyloid aggregation. Resistance of the prion forming domain (PFD) in Proteinase K proteolysis assays underlined that tannic acid favours amyloid fibre formation of HET-s.
Mona Boyé-Harnasch; Christophe Cullin
Related Documents :
16646524 - In vitro study of amp-deaminase from fish (cyprinus carpio) treated with hydrolyzable t...
12628514 - Mechanism-based in vitro screening of potential cancer chemopreventive agents.
8162174 - Drug competition for intracellular triiodothyronine-binding sites.
6163314 - Structure of the hair rootlets on cochlear sensory cells by tannic acid fixation.
12093284 - The biosynthetic incorporation of short-chain linear saturated fatty acids by acholepla...
1826504 - Column-friendly reversed-phase high-performance liquid chromatography of peptides and p...
Publication Detail:
Type:  Comparative Study; Journal Article; Research Support, Non-U.S. Gov't     Date:  2006-04-18
Journal Detail:
Title:  Journal of biotechnology     Volume:  125     ISSN:  0168-1656     ISO Abbreviation:  J. Biotechnol.     Publication Date:  2006 Sep 
Date Detail:
Created Date:  2006-08-14     Completed Date:  2006-10-03     Revised Date:  2006-11-15    
Medline Journal Info:
Nlm Unique ID:  8411927     Medline TA:  J Biotechnol     Country:  Netherlands    
Other Details:
Languages:  eng     Pagination:  222-30     Citation Subset:  IM    
Institut de Biochimie et Génétique Cellulaire, 1 rue Camille St Saëns, CNRS UMR 5095, 33077 Bordeaux Cedex, France.
Export Citation:
APA/MLA Format     Download EndNote     Download BibTex
MeSH Terms
Amyloid / biosynthesis,  drug effects,  metabolism*
Biotechnology / instrumentation,  methods*
Endopeptidase K / metabolism
Fungal Proteins / genetics,  isolation & purification,  metabolism
Microscopy, Electron
Microscopy, Fluorescence
Podospora / genetics,  metabolism
Prions / genetics,  isolation & purification,  metabolism*
Recombinant Proteins / isolation & purification,  metabolism
Tannins / pharmacology*
Reg. No./Substance:
0/Amyloid; 0/Fungal Proteins; 0/Prions; 0/Recombinant Proteins; 0/Tannins; EC K

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine

Previous Document:  Insights into extreme thermoacidophily based on genome analysis of Picrophilus torridus and other th...
Next Document:  Conventional gene targeting protocols lead to loss of targeted cells when applied to a silent gene l...