Self-assembly and anti-amyloid cytotoxicity activity of amyloid beta peptide derivatives

 |  Login

Show simple item record

dc.contributor Aalto-yliopisto fi
dc.contributor Aalto University en
dc.contributor.author Castelletto, V.
dc.contributor.author Ryumin, P.
dc.contributor.author Cramer, R.
dc.contributor.author Hamley, I. W.
dc.contributor.author Taylor, M.
dc.contributor.author Allsop, D.
dc.contributor.author Reza, M.
dc.contributor.author Ruokolainen, J.
dc.contributor.author Arnold, T.
dc.contributor.author Hermida-Merino, D.
dc.contributor.author Garcia, C. I.
dc.contributor.author Leal, M. C.
dc.contributor.author Castaño, E.
dc.date.accessioned 2017-03-28T12:14:12Z
dc.date.available 2017-03-28T12:14:12Z
dc.date.issued 2017-03-08
dc.identifier.citation Castelletto , V , Ryumin , P , Cramer , R , Hamley , I W , Taylor , M , Allsop , D , Reza , M , Ruokolainen , J , Arnold , T , Hermida-Merino , D , Garcia , C I , Leal , M C & Castaño , E 2017 , ' Self-assembly and anti-amyloid cytotoxicity activity of amyloid beta peptide derivatives ' Scientific Reports , vol 7 , 43637 , pp. 1-12 . DOI: 10.1038/srep43637 en
dc.identifier.issn 2045-2322
dc.identifier.other PURE UUID: e99ae9fc-8cef-4f34-80d9-cee803e557e1
dc.identifier.other PURE ITEMURL: https://research.aalto.fi/en/publications/selfassembly-and-antiamyloid-cytotoxicity-activity-of-amyloid-beta-peptide-derivatives(e99ae9fc-8cef-4f34-80d9-cee803e557e1).html
dc.identifier.other PURE LINK: http://www.scopus.com/inward/record.url?scp=85014918980&partnerID=8YFLogxK
dc.identifier.other PURE FILEURL: https://research.aalto.fi/files/11411450/srep43637.pdf
dc.identifier.uri https://aaltodoc.aalto.fi/handle/123456789/25029
dc.description.abstract The self-assembly of two derivatives of KLVFF, a fragment Aβ(16-20) of the amyloid beta (Aβ) peptide, is investigated and recovery of viability of neuroblastoma cells exposed to Aβ (1-42) is observed at sub-stoichiometric peptide concentrations. Fluorescence assays show that NH 2 -KLVFF-CONH 2 undergoes hydrophobic collapse and amyloid formation at the same critical aggregation concentration (cac). In contrast, NH 2 -K(Boc)LVFF-CONH 2 undergoes hydrophobic collapse at a low concentration, followed by amyloid formation at a higher cac. These findings are supported by the β-sheet features observed by FTIR. Electrospray ionization mass spectrometry indicates that NH 2 -K(Boc)LVFF-CONH 2 forms a significant population of oligomeric species above the cac. Cryo-TEM, used together with SAXS to determine fibril dimensions, shows that the length and degree of twisting of peptide fibrils seem to be influenced by the net peptide charge. Grazing incidence X-ray scattering from thin peptide films shows features of β-sheetordering for both peptides, along with evidence for lamellar ordering of NH 2 -KLVFF-CONH 2. This work provides a comprehensive picture of the aggregation properties of these two KLVFF derivatives and shows their utility, in unaggregated form, in restoring the viability of neuroblastoma cells against Aβ-induced toxicity. en
dc.format.extent 1-12
dc.format.mimetype application/pdf
dc.language.iso en en
dc.relation.ispartofseries Scientific Reports en
dc.relation.ispartofseries Volume 7 en
dc.rights openAccess en
dc.subject.other General en
dc.subject.other 114 Physical sciences en
dc.title Self-assembly and anti-amyloid cytotoxicity activity of amyloid beta peptide derivatives en
dc.type A1 Alkuperäisartikkeli tieteellisessä aikakauslehdessä fi
dc.description.version Peer reviewed en
dc.contributor.department University of Reading
dc.contributor.department Lancaster University
dc.contributor.department Department of Applied Physics
dc.contributor.department Diamond Light Source
dc.contributor.department ESRF-The European Synchrotron
dc.contributor.department Consejo Nacional de Investigaciones Científicas y Técnicas
dc.subject.keyword General
dc.subject.keyword 114 Physical sciences
dc.identifier.urn URN:NBN:fi:aalto-201703283268
dc.identifier.doi 10.1038/srep43637
dc.type.version publishedVersion


Files in this item

Files Size Format View

There are no files associated with this item.

This item appears in the following Collection(s)

Show simple item record

Search archive


Advanced Search

article-iconSubmit a publication

Browse

My Account