Abstract
Deposition of β-amyloid fibrils within senile plaques in the brain is a major hallmark of Alzheimer's disease. In this study, atomic force microscopy (AFM) has been used to provide surface topographical data of amyloid fibrillization as a function of pH. Alteration of pH has led to observed changes in fibril self-assembly rate, diameter and branching. These results suggest that pH has a profound affect on β-amyloid self-assembly and surface morphology.
Protein & Peptide Letters
Title:Molecular Surface Morphology Studies Of β-Amyloid Self-Assembly Effect of pH On Fibril Formation
Volume: 3 Issue: 6
Author(s): A.P. Shivji, M. C. Davies, C. J. Roberts, S. J. B. Tendler and M. J. Wilkinson
Affiliation:
Abstract: Deposition of β-amyloid fibrils within senile plaques in the brain is a major hallmark of Alzheimer's disease. In this study, atomic force microscopy (AFM) has been used to provide surface topographical data of amyloid fibrillization as a function of pH. Alteration of pH has led to observed changes in fibril self-assembly rate, diameter and branching. These results suggest that pH has a profound affect on β-amyloid self-assembly and surface morphology.
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Cite this article as:
Shivji A.P., Davies M. C., Roberts C. J., Tendler S. J. B. and Wilkinson M. J., Molecular Surface Morphology Studies Of β-Amyloid Self-Assembly Effect of pH On Fibril Formation, Protein & Peptide Letters 1996; 3 (6) . https://dx.doi.org/10.2174/092986650306221101124058
DOI https://dx.doi.org/10.2174/092986650306221101124058 |
Print ISSN 0929-8665 |
Publisher Name Bentham Science Publisher |
Online ISSN 1875-5305 |
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