sh.sePublications
Change search
CiteExportLink to record
Permanent link

Direct link
Cite
Citation style
  • apa
  • harvard1
  • ieee
  • modern-language-association-8th-edition
  • vancouver
  • Other style
More styles
Language
  • de-DE
  • en-GB
  • en-US
  • fi-FI
  • nn-NO
  • nn-NB
  • sv-SE
  • Other locale
More languages
Output format
  • html
  • text
  • asciidoc
  • rtf
Amyloid beta-peptide polymerization studied using fluorescence correlation spectroscopy
Show others and affiliations
1999 (English)In: Chemistry and Biology, ISSN 1074-5521, E-ISSN 1879-1301, Vol. 6, no 1, 53-62 p.Article in journal (Refereed) Published
Resource type
Text
Abstract [en]

Background: The accumulation of fibrillar deposits of amyloid beta-peptide (A beta) in brain parenchyma and cerebromeningeal blood vessels is a key step in the pathogenesis of Alzheimer's disease. In this report, polymerization of A beta was studied using fluorescence correlation spectroscopy (FCS), a technique capable of detecting small molecules and large aggregates simultaneously in solution. Results: The polymerization of A beta dissolved in Tris-buffered saline, pH 7.4, occurred above a critical concentration of 50 mu M and proceeded from monomers/dimers into two discrete populations of large aggregates, without any detectable amount of oligomers. The aggregation showed very high cooperativity and reached a maximum after 40 min, followed by an increase in the amount of monomers/dimers and a decrease in the size of the large aggregates. Electron micrographs of samples prepared at the time for maximum aggregation showed a mixture of an amorphous network and short diffuse fibrils, whereas only mature amyloid fibrils were detected after one day of incubation. The aggregation was reduced when A beta was incubated in the presence of A beta ligands, oligopeptides previously shown to inhibit fibril formation, and aggregates were partly dissociated after the addition of the ligands. Conclusions: The polymerization of A beta is a highly cooperative process in which the formation of very large aggregates precedes the formation of fibrils. The entire process can be inhibited and, at least in early stages, partly reversed by A beta ligands.

Place, publisher, year, edition, pages
1999. Vol. 6, no 1, 53-62 p.
Keyword [en]
aggregation properties, alzheimer's disease, amino-terminal fragment, amyloid beta-peptide, atomic-force microscopy, familial alzheimers-disease, fibril formation, fluorescence correlation spectroscopy, in-vitro, integral-equations, missense mutations, polymerization, precursor protein, transgenic mice
National Category
Biophysics
Identifiers
URN: urn:nbn:se:sh:diva-29040DOI: 10.1016/S1074-5521(99)80020-9ISI: 000082564500009PubMedID: 9889152OAI: oai:DiVA.org:sh-29040DiVA: diva2:891581
Note

Times Cited: 30 Article English Cited References Count: 58 235wa

Available from: 2016-01-07 Created: 2016-01-07 Last updated: 2016-01-08Bibliographically approved

Open Access in DiVA

No full text

Other links

Publisher's full textPubMed

Search in DiVA

By author/editor
Berndt, Kurt D
In the same journal
Chemistry and Biology
Biophysics

Search outside of DiVA

GoogleGoogle Scholar

Altmetric score

Total: 43 hits
CiteExportLink to record
Permanent link

Direct link
Cite
Citation style
  • apa
  • harvard1
  • ieee
  • modern-language-association-8th-edition
  • vancouver
  • Other style
More styles
Language
  • de-DE
  • en-GB
  • en-US
  • fi-FI
  • nn-NO
  • nn-NB
  • sv-SE
  • Other locale
More languages
Output format
  • html
  • text
  • asciidoc
  • rtf