Abstract
Kinetic behavior of aggregation of amyloid-β-protein (Aβ) is represented by a stretched exponential function, F=A{1-exp(-Btn)}. Differences in temperature-dependence of A, B and n are studied for Aβ 1-40 and Aβ 1-42. As the temperature is lowered, parameter A is increased, parameter B is decreased and parameter n is increased in Aβ 1-40, while these parameters are less sensitive to temperature in a more hydrophobic protein Aβ 1-42. ln B is a linear function of n, which is shown by ln B = -6.34n + 3.69.
Keywords: fibril formation, amyloid-b-protein, stretched exponential function, hydrophobic protein
Protein & Peptide Letters
Title: Analysis of Fibril Formation of Amyloid-β- Protein by Stretched Exponential Function
Volume: 10 Issue: 6
Author(s): Ken-ichi Shinozaki, Takeo Konakahara, Hiroaki Okuno and Masato Kodaka
Affiliation:
Keywords: fibril formation, amyloid-b-protein, stretched exponential function, hydrophobic protein
Abstract: Kinetic behavior of aggregation of amyloid-β-protein (Aβ) is represented by a stretched exponential function, F=A{1-exp(-Btn)}. Differences in temperature-dependence of A, B and n are studied for Aβ 1-40 and Aβ 1-42. As the temperature is lowered, parameter A is increased, parameter B is decreased and parameter n is increased in Aβ 1-40, while these parameters are less sensitive to temperature in a more hydrophobic protein Aβ 1-42. ln B is a linear function of n, which is shown by ln B = -6.34n + 3.69.
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Cite this article as:
Shinozaki Ken-ichi, Konakahara Takeo, Okuno Hiroaki and Kodaka Masato, Analysis of Fibril Formation of Amyloid-β- Protein by Stretched Exponential Function, Protein & Peptide Letters 2003; 10 (6) . https://dx.doi.org/10.2174/0929866033478582
DOI https://dx.doi.org/10.2174/0929866033478582 |
Print ISSN 0929-8665 |
Publisher Name Bentham Science Publisher |
Online ISSN 1875-5305 |
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