Issue 58, 2013
From the journal:

Chemical Communications

Human lysozyme inhibits the in vitro aggregation of Aβ peptides, which in vivo are associated with Alzheimer's disease†

Jinghui Luo,a   Sebastian K. T. S. Wärmländer,b   Astrid Gräslundb  and  Jan Pieter Abrahams*a  

* Corresponding authors

a Gorlaeus Laboratory, Leiden Institute of Chemistry, Leiden University, 2300RA Leiden, The Netherlands

b Department of Biochemistry and Biophysics, Stockholm University, SE-10691 Stockholm, Sweden
E-mail: Abrahams@chem.leidenuniv.nl

Abstract

Alzheimer's disease is a neurodegenerative disorder characterized by accumulation of Aβ peptide aggregates in the brain. Using ThT fluorescence assays, AFM imaging, NMR and CD spectroscopy, and MD modeling we show that lysozyme – a hydrolytic enzyme abundant in human secretions – completely inhibits the aggregation of Aβ peptides at equimolar lysozyme : Aβ peptide ratios.

Graphical abstract: Human lysozyme inhibits the in vitro aggregation of Aβ peptides, which in vivo are associated with Alzheimer's disease

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Article information

DOI
https://doi.org/10.1039/C3CC42325E
Article type
Communication
Submitted
30 Mar 2013
Accepted
29 May 2013
First published
29 May 2013

Chem. Commun., 2013,49, 6507-6509

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Human lysozyme inhibits the in vitro aggregation of Aβ peptides, which in vivo are associated with Alzheimer's disease

J. Luo, S. K. T. S. Wärmländer, A. Gräslund and J. P. Abrahams, Chem. Commun., 2013, 49, 6507 DOI: 10.1039/C3CC42325E

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