| Shear-flow induced changes in apolipoprotein C-II conformation and amyloid fibril formation. | |
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MedLine Citation:
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PMID: 21476595 Owner: NLM Status: Publisher |
Abstract/OtherAbstract:
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The misfolding and self-assembly of proteins into amyloid fibrils that occurs in several debilitating diseases is affected by a variety of environmental factors including mechanical factors associated with shear flow. We examined the effects of shear flow on amyloid fibril formation by human apolipoprotein (apo) C-II. Shear fields, 150 s-1, 300 s-1 and 500 s-1, accelerated the rate of apoC-II fibril formation (1 mg/ml) approximately 5 - 10 fold. Fibrils produced at shear rates of 150 s-1 and 300 s-1 were similar to the twisted ribbon fibrils formed in the absence of shear, while at 500 s-1, tangled rope-like structures were observed. The mechanism of the shear-induced acceleration of amyloid fibril formation was investigated at low apoC-II concentrations (50 µg/ml) where fibril formation does not occur. Circular dichroism and tryptophan fluorescence indicated that shear induced an irreversible change in apoC-II secondary structure. Fluorescence resonance energy transfer experiments using the single tryptophan residue in apoC-II as the donor and covalently attached acceptors showed that shear flow increased the distance between the donor and acceptor molecules. Shear-induced higher oligomeric species were identified by sedimentation velocity experiments using fluorescence detection, while fibril seeding experiments showed that species formed during shear-flow are on the fibril formation pathway. These studies suggest that physiological shear-flow conditions and conditions experienced during protein manufacturing can exert significant effects on protein conformation leading to protein misfolding, aggregation, and amyloid fibril formation. |
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Authors:
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Chai Lean Teoh; Innocent B Bekard; Peter Asimakis; Michael D W Griffin; Timothy W Ryan; Dave Edwin Dunstan; Geoffrey John Howlett |
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Publication Detail:
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Type: JOURNAL ARTICLE Date: 2011-4-9 |
Journal Detail:
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Title: Biochemistry Volume: - ISSN: 1520-4995 ISO Abbreviation: - Publication Date: 2011 Apr |
Date Detail:
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Created Date: 2011-4-11 Completed Date: - Revised Date: - |
Medline Journal Info:
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Nlm Unique ID: 0370623 Medline TA: Biochemistry Country: - |
Other Details:
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Languages: ENG Pagination: - Citation Subset: - |
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From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine
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