The role of protonation in protein fibrillation

Martin Jeppesen, Peter Westh, Daniel Otzen

Publikation: Bidrag til tidsskriftTidsskriftartikelForskningpeer review

Resumé

Many proteins fibrillate at low pH despite a high population of charged side chains. Therefore exchange of protons between the fibrillating peptide and its surroundings may play an important role in fibrillation. Here, we use isothermal titration calorimetry to measure exchange of protons between buffer and the peptide hormone glucagon during fibrillation. Glucagon absorbs or releases protons to an extent which allows it to attain a net charge of zero in the fibrillar state, both at acidic and basic pH. Similar results are obtained for lysozyme. This suggests that side chain pKa values change dramatically in the fibrillar state.
OriginalsprogEngelsk
TidsskriftFEBS Letters
Vol/bind584
Udgave nummer4
Sider (fra-til)780-784
ISSN0014-5793
DOI
StatusUdgivet - 2010

Emneord

    Citer dette

    Jeppesen, Martin ; Westh, Peter ; Otzen, Daniel. / The role of protonation in protein fibrillation. I: FEBS Letters. 2010 ; Bind 584, Nr. 4. s. 780-784.
    @article{58a5441013d211df9bed000ea68e967b,
    title = "The role of protonation in protein fibrillation",
    abstract = "Many proteins fibrillate at low pH despite a high population of charged side chains. Therefore exchange of protons between the fibrillating peptide and its surroundings may play an important role in fibrillation. Here, we use isothermal titration calorimetry to measure exchange of protons between buffer and the peptide hormone glucagon during fibrillation. Glucagon absorbs or releases protons to an extent which allows it to attain a net charge of zero in the fibrillar state, both at acidic and basic pH. Similar results are obtained for lysozyme. This suggests that side chain pKa values change dramatically in the fibrillar state.",
    keywords = "Fibrillation, protonation, glucagon, elongation",
    author = "Martin Jeppesen and Peter Westh and Daniel Otzen",
    year = "2010",
    doi = "10.1016/j.febslet.2010.01.002",
    language = "English",
    volume = "584",
    pages = "780--784",
    journal = "F E B S Letters",
    issn = "0014-5793",
    publisher = "JohnWiley & Sons Ltd.",
    number = "4",

    }

    The role of protonation in protein fibrillation. / Jeppesen, Martin; Westh, Peter; Otzen, Daniel.

    I: FEBS Letters, Bind 584, Nr. 4, 2010, s. 780-784.

    Publikation: Bidrag til tidsskriftTidsskriftartikelForskningpeer review

    TY - JOUR

    T1 - The role of protonation in protein fibrillation

    AU - Jeppesen, Martin

    AU - Westh, Peter

    AU - Otzen, Daniel

    PY - 2010

    Y1 - 2010

    N2 - Many proteins fibrillate at low pH despite a high population of charged side chains. Therefore exchange of protons between the fibrillating peptide and its surroundings may play an important role in fibrillation. Here, we use isothermal titration calorimetry to measure exchange of protons between buffer and the peptide hormone glucagon during fibrillation. Glucagon absorbs or releases protons to an extent which allows it to attain a net charge of zero in the fibrillar state, both at acidic and basic pH. Similar results are obtained for lysozyme. This suggests that side chain pKa values change dramatically in the fibrillar state.

    AB - Many proteins fibrillate at low pH despite a high population of charged side chains. Therefore exchange of protons between the fibrillating peptide and its surroundings may play an important role in fibrillation. Here, we use isothermal titration calorimetry to measure exchange of protons between buffer and the peptide hormone glucagon during fibrillation. Glucagon absorbs or releases protons to an extent which allows it to attain a net charge of zero in the fibrillar state, both at acidic and basic pH. Similar results are obtained for lysozyme. This suggests that side chain pKa values change dramatically in the fibrillar state.

    KW - Fibrillation

    KW - protonation

    KW - glucagon

    KW - elongation

    U2 - 10.1016/j.febslet.2010.01.002

    DO - 10.1016/j.febslet.2010.01.002

    M3 - Journal article

    VL - 584

    SP - 780

    EP - 784

    JO - F E B S Letters

    JF - F E B S Letters

    SN - 0014-5793

    IS - 4

    ER -