Change search
CiteExportLink to record
Permanent link

Direct link
Cite
Citation style
  • apa
  • 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
Inhibiting and Reversing Amyloid-β Peptide (1-40) Fibril Formation with Gramicidin S and Engineered Analogues
Stockholm University, Faculty of Science, Department of Biochemistry and Biophysics.
Show others and affiliations
2013 (English)In: Chemistry - A European Journal, ISSN 0947-6539, E-ISSN 1521-3765, Vol. 19, no 51, 17338-17348 p.Article in journal (Refereed) Published
Abstract [en]

In Alzheimer's disease, amyloid-β (Aβ) peptides aggregate into extracellular fibrillar deposits. Although these deposits may not be the prime cause of the neurodegeneration that characterizes this disease, inhibition or dissolution of amyloid fibril formation by Aβ peptides is likely to affect its development. ThT fluorescence measurements and AFM images showed that the natural antibiotic gramicidin S significantly inhibited Aβ amyloid formation in vitro and could dissolve amyloids that had formed in the absence of the antibiotic. In silico docking suggested that gramicidin S, a cyclic decapeptide that adopts a β-sheet conformation, binds to the Aβ peptide hairpin-stacked fibril through β-sheet interactions. This may explain why gramicidin S reduces fibril formation. Analogues of gramicidin S were also tested. An analogue with a potency that was four-times higher than that of the natural product was identified.

Place, publisher, year, edition, pages
2013. Vol. 19, no 51, 17338-17348 p.
Keyword [en]
Alzheimer’s disease, amyloid-beta peptides, antibiotics, fibrillization, structure–activity relationships
National Category
Biochemistry and Molecular Biology
Identifiers
URN: urn:nbn:se:su:diva-98629DOI: 10.1002/chem.201301535ISI: 000327889800015PubMedID: 24218178OAI: oai:DiVA.org:su-98629DiVA: diva2:684684
Funder
Swedish Research Council
Note

Funding agencies:

NOW top grant; Swedish Research Council; Xunta de Galicia Angeles Alvarino fellowship; European Social Fund 

Available from: 2014-01-08 Created: 2014-01-08 Last updated: 2017-12-06Bibliographically approved

Open Access in DiVA

No full text

Other links

Publisher's full textPubMed

Search in DiVA

By author/editor
Wärmländer, Sebastian K T SGräslund, Astrid
By organisation
Department of Biochemistry and Biophysics
In the same journal
Chemistry - A European Journal
Biochemistry and Molecular Biology

Search outside of DiVA

GoogleGoogle Scholar

doi
pubmed
urn-nbn

Altmetric score

doi
pubmed
urn-nbn
Total: 24 hits
CiteExportLink to record
Permanent link

Direct link
Cite
Citation style
  • apa
  • 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