2010 Fiscal Year Final Research Report
Position Effects in Amyloid Kinetics
| Project/Area Number |
21770103
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| Research Category |
Grant-in-Aid for Young Scientists (B)
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| Allocation Type | Single-year Grants |
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| Research Field |
Structural biochemistry
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| Research Institution | University of Tsukuba |
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Principal Investigator |
HALL Damien University of Tsukuba, 大学院・人間総合科学研究科, 助教 (50447950)
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| Project Period (FY) |
2009 – 2010
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| Keywords | アルツハイマー病 / アミロイド仮説 / アミロイドの速度論 / アミロイドの位置効果 / アミロイドの形成と解離 |
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| Research Abstract |
2009-Position Effects in the Breakage of an Amyloid Fiber : In the first year we used a series of model peptides and polypeptides to make amyloid fibers under controlled in vitro conditions. These fibers were broken by use of either applied shearing force (flow or applied sonic pulse) or by heating under solvent conditions that favored dissolution of the fiber. The broken fibers were then analyzed by transmission electron microscopy (TEM) and a length distribution recorded. Computer models were developed for both the interpretation of the assay results and for first principles prediction of the breakage pattern of the amyloid fibers. 2010-Position Effects in the Propensity of a Peptide to Form Amyloid: In the second year we sought to examine the effect of positional placement of a peptide segment in a larger polymer sequence on the rate of the amyloid growth kinetics. We spent some time testing and refining procedures for performing the characterization of size distributions. We developed novel assay formats based on size-exclusion chromatography (SEC), transmission electron microscopy (TEM), densitometry of conventional SDS gel-electrophoresis (GE) experiments and a functional assay for determining the chemical reactivity of the surface based on a time dependent ligand binding assay.
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