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The role of histidines in amyloid β fibril assembly.
Umeå University, Faculty of Medicine, Department of Medical Biochemistry and Biophysics.
Umeå University, Faculty of Medicine, Department of Medical Biochemistry and Biophysics.
Umeå University, Faculty of Medicine, Department of Molecular Biology (Faculty of Medicine).
Umeå University, Faculty of Medicine, Department of Medical Biochemistry and Biophysics.
2017 (English)In: FEBS Letters, ISSN 0014-5793, E-ISSN 1873-3468Article in journal (Refereed) Epub ahead of print
Abstract [en]

Low pH has a strong stabilising effect on the fibrillar assembly of amyloid β, which is associated with Alzheimer's disease. The stabilising effect is already pronounced at pH 6.0, suggesting that protonation of histidines might mediate this effect. Through the systematic substitution of the three native histidines in Aβ for alanines, we have evaluated their role in fibril stability. Using surface plasmon resonance, we show that at neutral pH the fibrillar forms of all His-Ala variants are destabilised by a factor of 4-12 compared to wild-type Aβ. However, none of the His-Ala Aβ variants impair the stabilising effect of the fibril at low pH.

Place, publisher, year, edition, pages
2017.
Keyword [en]
abeta, amyloid, fibril, histidine, stability, surface plasmon resonance
National Category
Medical Biotechnology (with a focus on Cell Biology (including Stem Cell Biology), Molecular Biology, Microbiology, Biochemistry or Biopharmacy)
Identifiers
URN: urn:nbn:se:umu:diva-133486DOI: 10.1002/1873-3468.12616PubMedID: 28267202OAI: oai:DiVA.org:umu-133486DiVA: diva2:1087869
Available from: 2017-04-10 Created: 2017-04-10 Last updated: 2017-04-10

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Brännström, KristofferIslam, TohidulSandblad, LindaOlofsson, Anders
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Department of Medical Biochemistry and BiophysicsDepartment of Molecular Biology (Faculty of Medicine)
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Medical Biotechnology (with a focus on Cell Biology (including Stem Cell Biology), Molecular Biology, Microbiology, Biochemistry or Biopharmacy)

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Citation style
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  • Other locale
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