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Protein & Peptide Letters

Editor-in-Chief

ISSN (Print): 0929-8665
ISSN (Online): 1875-5305

Review Article

Molecular Surface Morphology Studies Of β-Amyloid Self-Assembly Effect of pH On Fibril Formation

Author(s): A.P. Shivji, M. C. Davies, C. J. Roberts, S. J. B. Tendler and M. J. Wilkinson

Volume 3, Issue 6, 1996

Page: [407 - 414] Pages: 8

DOI: 10.2174/092986650306221101124058

Price: $65

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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