Effect of dendrimers on pure acetylcholinesterase activity and structure

The effect of polyamidoamine (PAMAM) dendrimers on activity and fluorescence of pure acetylcholinesterase (EC 3.1.1.7.) was studied. It has been shown that all dendrimers studied decreased the enzymatic activity of acetylcholinesterase. This effect depended on the type of dendrimers. The data on the...

Full description

Saved in:
Bibliographic Details
Published in:Bioelectrochemistry (Amsterdam, Netherlands) Netherlands), 2006, Vol.68 (1), p.56-59
Main Authors: Shcharbin, D., Jokiel, M., Klajnert, B., Bryszewska, M.
Format: Article
Language:English
Subjects:
Acetylcholinesterase
Acetylcholinesterase - chemistry
Acetylcholinesterase - metabolism
Conformation
Dendrimers - chemistry
Dendrimers - pharmacology
Enzyme activity
Fluorescence
PAMAM dendrimer
Protein Conformation - drug effects
Spectrometry, Fluorescence
Citations: Items that this one cites
Items that cite this one
Online Access:Get full text
Tags: Add Tag
No Tags, Be the first to tag this record!
Description
Summary:The effect of polyamidoamine (PAMAM) dendrimers on activity and fluorescence of pure acetylcholinesterase (EC 3.1.1.7.) was studied. It has been shown that all dendrimers studied decreased the enzymatic activity of acetylcholinesterase. This effect depended on the type of dendrimers. The data on the intrinsic fluorescence have shown that the dendrimers changed acetylcholinesterase conformation and the strongest effect was induced by PAMAM G3.5 dendrimer.
ISSN:1567-5394
DOI:10.1016/j.bioelechem.2005.04.001