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Updated: Jul 17, 2026

Analysis of β-Amyloid-induced Abnormalities on Fibrin Clot Structure by Spectroscopy and Scanning Electron Microscopy
Published on: November 30, 2018
Analysis of fibril formation of amyloid-beta-protein by stretched exponential function
Ken-ichi Shinozaki1, Takeo Konakahara, Hiroaki Okuno
1Institute for Biological Resources and Functions, National Institute of Advanced Industrial Science and Technology (AIST), Tsukuba, Japan.
Abstract:
Kinetic behavior of aggregation of amyloid-beta-protein (Abeta) is represented by a stretched exponential function, F=A[1-exp(-Bt(n))]. Differences in temperature-dependence of A, B and n are studied for Abeta 1-40 and Abeta 1-42. As the temperature is lowered, parameter A is increased, parameter B is decreased and parameter n is increased in Abeta 1-40, while these parameters are less sensitive to temperature in a more hydrophobic protein Abeta 1-42. ln B is a linear function of n, which is shown by ln B = -6.34n + 3.69.
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