onr:"swepub:oai:DiVA.org:su-131935"
Search: onr:"swepub:oai:DiVA.org:su-131935" > Ionic Strength Modu...
- 1 of 1
- Previous record
- Next record
- To hitlist
- Abelein, AxelStockholms universitet,Institutionen för biokemi och biofysik (author)
Ionic Strength Modulation of the Free Energy Landscape of A beta(40) Peptide Fibril Formation
- Article/chapterEnglish2016
Publisher, publication year, extent ...
- 2016-05-23
- American Chemical Society (ACS),2016
- printrdacarrier
Numbers
- LIBRIS-ID:oai:DiVA.org:su-131935
- https://urn.kb.se/resolve?urn=urn:nbn:se:su:diva-131935URI
- https://doi.org/10.1021/jacs.6b04511DOI
- http://kipublications.ki.se/Default.aspx?queryparsed=id:133675024URI
Supplementary language notes
- Language:English
- Summary in:English
Part of subdatabase
- SwePubSwePub
Classification
Notes
- Protein misfolding and formation of cross-beta structured amyloid fibrils are linked to, many neurodegenerative disorders. Although recently developed,quantitative approaches have started to reveal the molecular nature of self-assembly and fibril formation of proteins and peptides, it is yet unclear how these self-organization events are precisely modulated by microenvironmental factors, which are known to strongly affect the macroscopic aggregation properties. Here, we characterize the explicit effect of ionic strength on the microscopic aggregation rates of amyloid beta peptide (A beta 40) self-association, implicated in Alzheimer's disease. We found that physiological ionic strength accelerates A beta 40 aggregation kinetics by promoting surface-catalyzed secondary nucleation reactions. This promoted catalytic effect can be assigned to shielding of electrostatic repulsion between Monomers on the fibril surface or between the fibril surface itself and monomeric peptides. Furthermore, we observe the formation of two different beta-structured states with =similar but distinct spectroscopic features, which can be assigned to an off-pathway immature state (F-beta*) and a mature stable State (F-beta), where salt favors formation of the F-beta fibril morphology. Addition of salt to preformed F-beta* accelerates transition to F-beta, underlining the dynamic nature of A beta 40 fibrils in solution. On the basis of,these results we suggest a model where salt decreases the free-energy barrier for A beta 40 folding to the F-beta state, favoring the buildup of the mature fibril morphology while omitting competing, energetically less favorable structural states.
Subject headings and genre
- NATURVETENSKAP Kemi hsv//swe
- NATURAL SCIENCES Chemical Sciences hsv//eng
Added entries (persons, corporate bodies, meetings, titles ...)
- Jarvet, JüriStockholms universitet,Institutionen för biokemi och biofysik,The National Institute of Chemical Physics and Biophysics, Estonia(Swepub:su)jyri (author)
- Barth, AndreasStockholms universitet,Institutionen för biokemi och biofysik(Swepub:su)abart (author)
- Gräslund, AstridStockholms universitet,Institutionen för biokemi och biofysik(Swepub:su)astrid (author)
- Danielsson, JensStockholms universitet,Institutionen för biokemi och biofysik(Swepub:su)jedan (author)
- Stockholms universitetInstitutionen för biokemi och biofysik (creator_code:org_t)
Related titles
- In:Journal of the American Chemical Society: American Chemical Society (ACS)138:21, s. 6893-69020002-78631520-5126
Internet link
Find in a library
- Journal of the American Chemical Society (Search for host publication in LIBRIS)
To the university's database
- 1 of 1
- Previous record
- Next record
- To hitlist
Find more in SwePub
- By the author/editor
- Abelein, Axel
- Jarvet, Jüri
- Barth, Andreas
- Gräslund, Astrid
- Danielsson, Jens
- About the subject
-
- NATURAL SCIENCES
- NATURAL SCIENCES
- and Chemical Science ...
- Articles in the publication
- Journal of the A ...
- By the university
- Stockholm University
- Karolinska Institutet
Search outside SwePub
- Extend your search to:
- Google Book Search
- Google Scholar
Kungliga biblioteket hanterar dina personuppgifter i enlighet med EU:s dataskyddsförordning (2018), GDPR. Läs mer om hur det funkar här.
Så här hanterar KB dina uppgifter vid användning av denna tjänst.
- Copyright © LIBRIS - National Library Systems
- LIBRIS.kb.se
