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Analysis of Fibril Formation of Amyloid-β- Protein by Stretched Exponential Function

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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: amyloid-b-protein; fibril formation; hydrophobic protein; stretched exponential function

Document Type: Review Article


Affiliations: Institute for Biological Resources and Functions, National Institute of Advanced Industrial Science and Technology (AIST), Tsukuba Central 6, 1-1-1 Higashi, Tsukuba, Ibaraki 305-8566, Japan.

Publication date: December 1, 2003

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  • Protein & Peptide Letters publishes short papers in all important aspects of protein and peptide research, including structural studies, recombinant expression, function, synthesis, enzymology, immunology, molecular modeling, drug design etc. Manuscripts must have a significant element of novelty, timeliness and urgency that merit rapid publication. Reports of crystallisation, and preliminary structure determinations of biologically important proteins are acceptable. Purely theoretical papers are also acceptable provided they provide new insight into the principles of protein/peptide structure and function.

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