You are not logged in.

Phosphate and HEPES buffers potently affect the fibrillation and oligomerization mechanism of Alzheimer’s Aβ peptide

Garvey, Megan, Tepper, Katharina, Haupt, Caroline, Knüpfer, Uwe, Klement, Karolin, Meinhardt, Jessica, Horn, Uwe, Balbach, Jochen and Fändrich, Marcus 2011, Phosphate and HEPES buffers potently affect the fibrillation and oligomerization mechanism of Alzheimer’s Aβ peptide, Biochemical and biophysical research communications, vol. 409, no. 3, pp. 385-388, doi: 10.1016/j.bbrc.2011.04.141.

Attached Files
Name Description MIMEType Size Downloads

Title Phosphate and HEPES buffers potently affect the fibrillation and oligomerization mechanism of Alzheimer’s Aβ peptide
Author(s) Garvey, Megan
Tepper, Katharina
Haupt, Caroline
Knüpfer, Uwe
Klement, Karolin
Meinhardt, Jessica
Horn, Uwe
Balbach, Jochen
Fändrich, Marcus
Journal name Biochemical and biophysical research communications
Volume number 409
Issue number 3
Start page 385
End page 388
Total pages 4
Publisher Elsevier
Place of publication Amsterdam, The Netherlands
Publication date 2011-06-10
ISSN 0006-291X
Keyword(s) Amyloid

Buffer system
Fibrillation
oligomerization
Alzheimer’s Aβ peptide
Alzheimer’s disease
Summary The oligomerization of Aβ peptide into amyloid fibrils is a hallmark of Alzheimer’s disease. Due to its biological relevance, phosphate is the most commonly used buffer system for studying the formation of Aβ and other amyloid fibrils. Investigation into the characteristics and formation of amyloid fibrils frequently relies upon material formed in vitro, predominantly in phosphate buffers. Herein, we examine the effects on the fibrillation and oligomerization mechanism of Aβ peptide that occur due solely to the influence of phosphate buffer. We reveal that significant differences in amyloid fibrillation are observed due to fibrillation being initiated in phosphate or HEPES buffer (at physiological pH and temperature). Except for the differing buffer ions, all experimental parameters were kept constant. Fibril formation was assessed using fluorescently monitored kinetic studies, microscopy, X-ray fiber diffraction and infrared and nuclear magnetic resonance spectroscopies. Based on this set up, we herein reveal profound effects on the mechanism and speed of Aβ fibrillation. The three histidine residues at positions 6, 13 and 14 of Aβ(1–40) are instrumental in these mechanistic changes. We conclude that buffer plays a more significant role in fibril formation than has been generally acknowledged.
Language eng
DOI 10.1016/j.bbrc.2011.04.141
Field of Research 110199 Medical Biochemistry and Metabolomics not elsewhere classified
0304 Medicinal And Biomolecular Chemistry
0601 Biochemistry And Cell Biology
1101 Medical Biochemistry And Metabolomics
Socio Economic Objective 970111 Expanding Knowledge in the Medical and Health Sciences
HERDC Research category C1.1 Refereed article in a scholarly journal
ERA Research output type C Journal article
Copyright notice ©2011, Elsevier Inc.
Persistent URL http://hdl.handle.net/10536/DRO/DU:30075473

Document type: Journal Article
Collections: Faculty of Health
School of Medicine
Connect to link resolver
 
Unless expressly stated otherwise, the copyright for items in DRO is owned by the author, with all rights reserved.

Versions
Version Filter Type
Citation counts: TR Web of Science Citation Count  Cited 13 times in TR Web of Science
Scopus Citation Count Cited 0 times in Scopus
Google Scholar Search Google Scholar
Access Statistics: 4 Abstract Views, 2 File Downloads  -  Detailed Statistics
Created: Tue, 28 Mar 2017, 15:12:20 EST

Every reasonable effort has been made to ensure that permission has been obtained for items included in DRO. If you believe that your rights have been infringed by this repository, please contact drosupport@deakin.edu.au.