The role of protonation in protein fibrillation

Martin Jeppesen, Peter Westh, Daniel Otzen

Research output: Contribution to journalJournal articleResearchpeer-review

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.

Original languageEnglish
JournalFEBS Letters
Volume584
Issue number4
Pages (from-to)780-784
ISSN0014-5793
DOIs
Publication statusPublished - 2010

Keywords

  • Fibrillation
  • protonation
  • glucagon
  • elongation

Cite this

Jeppesen, Martin ; Westh, Peter ; Otzen, Daniel. / The role of protonation in protein fibrillation. In: FEBS Letters. 2010 ; Vol. 584, No. 4. pp. 780-784.
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The role of protonation in protein fibrillation. / Jeppesen, Martin; Westh, Peter; Otzen, Daniel.

In: FEBS Letters, Vol. 584, No. 4, 2010, p. 780-784.

Research output: Contribution to journalJournal articleResearchpeer-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

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ER -