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Shear flow promotes amyloid-β fibrilization.

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Title: Shear flow promotes amyloid-β fibrilization.
Authors: Dunstan, Dave E.1 davided@unimelb.edu.au, Hamilton-Brown, Paul1, Asimakis, Peter1, Ducker, William1, Bertolini, Joseph2
Source: PEDS: Protein Engineering, Design & Selection. Dec2009, Vol. 22 Issue 12, p741-746. 6p. 2 Black and White Photographs, 3 Graphs.
Subjects: Amyloid beta-protein, Atomic force microscopy, Molecules, Proteins, Alzheimer's disease
Abstract: The rate of formation of amyloid fibrils in an aqueous solution of amyloid-β (Aβ) is greatly increased when the solution is sheared. When Aβ solution is stirred with a magnetic stirrer bar at 37°C, a rapid increase in thioflavin T fluorescence is observed. Atomic Force Microscopy (AFM) images show the formation of aggregates, the growth of fibrils and the intertwining of the fibrils with time. Circular dichroism (CD) spectroscopy of samples taken after stirring shows a transition from random coil to α-helix to β-sheet secondary structure over 20 h at 37°C. The fluorescence, AFM and CD measurements are all consistent with the formation of amyloid fibrils. Quiescent, non-stirred solutions incubated at 37°C showed no evidence of amyloid formation over a period of 3 days. Couette flow was found to accelerate the formation of amyloid fibrils demonstrating that the primary effect of stirring is not mixing but shearing. Only very small shear forces are applied to individual molecules in our experiments. Simple calculation suggests that the force is too small to support a hypothesis that shearing promotes partial unfolding of the protein as is observed. [ABSTRACT FROM PUBLISHER]
Copyright of PEDS: Protein Engineering, Design & Selection is the property of Oxford University Press / USA and its content may not be copied or emailed to multiple sites without the copyright holder's express written permission. Additionally, content may not be used with any artificial intelligence tools or machine learning technologies. However, users may print, download, or email articles for individual use. This abstract may be abridged. No warranty is given about the accuracy of the copy. Users should refer to the original published version of the material for the full abstract. (Copyright applies to all Abstracts.)
Database: Engineering Source
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DbLabel: Engineering Source
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  Data: Shear flow promotes amyloid-β fibrilization.
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  Data: <searchLink fieldCode="AR" term="%22Dunstan%2C+Dave+E%2E%22">Dunstan, Dave E.</searchLink><relatesTo>1</relatesTo><i> davided@unimelb.edu.au</i><br /><searchLink fieldCode="AR" term="%22Hamilton-Brown%2C+Paul%22">Hamilton-Brown, Paul</searchLink><relatesTo>1</relatesTo><br /><searchLink fieldCode="AR" term="%22Asimakis%2C+Peter%22">Asimakis, Peter</searchLink><relatesTo>1</relatesTo><br /><searchLink fieldCode="AR" term="%22Ducker%2C+William%22">Ducker, William</searchLink><relatesTo>1</relatesTo><br /><searchLink fieldCode="AR" term="%22Bertolini%2C+Joseph%22">Bertolini, Joseph</searchLink><relatesTo>2</relatesTo>
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  Data: <searchLink fieldCode="JN" term="%22PEDS%3A+Protein+Engineering%2C+Design+%26+Selection%22">PEDS: Protein Engineering, Design & Selection</searchLink>. Dec2009, Vol. 22 Issue 12, p741-746. 6p. 2 Black and White Photographs, 3 Graphs.
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  Data: <searchLink fieldCode="DE" term="%22Amyloid+beta-protein%22">Amyloid beta-protein</searchLink><br /><searchLink fieldCode="DE" term="%22Atomic+force+microscopy%22">Atomic force microscopy</searchLink><br /><searchLink fieldCode="DE" term="%22Molecules%22">Molecules</searchLink><br /><searchLink fieldCode="DE" term="%22Proteins%22">Proteins</searchLink><br /><searchLink fieldCode="DE" term="%22Alzheimer's+disease%22">Alzheimer's disease</searchLink>
– Name: Abstract
  Label: Abstract
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  Data: The rate of formation of amyloid fibrils in an aqueous solution of amyloid-β (Aβ) is greatly increased when the solution is sheared. When Aβ solution is stirred with a magnetic stirrer bar at 37°C, a rapid increase in thioflavin T fluorescence is observed. Atomic Force Microscopy (AFM) images show the formation of aggregates, the growth of fibrils and the intertwining of the fibrils with time. Circular dichroism (CD) spectroscopy of samples taken after stirring shows a transition from random coil to α-helix to β-sheet secondary structure over 20 h at 37°C. The fluorescence, AFM and CD measurements are all consistent with the formation of amyloid fibrils. Quiescent, non-stirred solutions incubated at 37°C showed no evidence of amyloid formation over a period of 3 days. Couette flow was found to accelerate the formation of amyloid fibrils demonstrating that the primary effect of stirring is not mixing but shearing. Only very small shear forces are applied to individual molecules in our experiments. Simple calculation suggests that the force is too small to support a hypothesis that shearing promotes partial unfolding of the protein as is observed. [ABSTRACT FROM PUBLISHER]
– Name: AbstractSuppliedCopyright
  Label:
  Group: Ab
  Data: <i>Copyright of PEDS: Protein Engineering, Design & Selection is the property of Oxford University Press / USA and its content may not be copied or emailed to multiple sites without the copyright holder's express written permission. Additionally, content may not be used with any artificial intelligence tools or machine learning technologies. However, users may print, download, or email articles for individual use. This abstract may be abridged. No warranty is given about the accuracy of the copy. Users should refer to the original published version of the material for the full abstract.</i> (Copyright applies to all Abstracts.)
PLink https://search.ebscohost.com/login.aspx?direct=true&site=eds-live&db=egs&AN=47429615
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      – Type: doi
        Value: 10.1093/protein/gzp059
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      – Code: eng
        Text: English
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        PageCount: 6
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      – SubjectFull: Amyloid beta-protein
        Type: general
      – SubjectFull: Atomic force microscopy
        Type: general
      – SubjectFull: Molecules
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      – SubjectFull: Proteins
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      – SubjectFull: Alzheimer's disease
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      – TitleFull: Shear flow promotes amyloid-β fibrilization.
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            NameFull: Hamilton-Brown, Paul
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            NameFull: Asimakis, Peter
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            NameFull: Ducker, William
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            NameFull: Bertolini, Joseph
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              M: 12
              Text: Dec2009
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              Y: 2009
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