Aarhus University Seal

The role of protonation in protein fibrillation

Research output: Contribution to journal/Conference contribution in journal/Contribution to newspaperJournal articleResearchpeer-review

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 pK(a) values change dramatically in the fibrillar state.
Original languageEnglish
JournalFEBS Letters
Pages (from-to)780-4
Number of pages5
Publication statusPublished - 19 Feb 2010

    Research areas

  • Buffers, Calorimetry, Circular Dichroism, Glucagon, Hydrogen-Ion Concentration, Kinetics, Microscopy, Atomic Force, Models, Chemical, Muramidase, Protein Folding, Proteins, Protons, Thermodynamics, Titrimetry

See relations at Aarhus University Citationformats

ID: 34567518