The role of protonation in protein fibrillation

Martin D Jeppesen; Peter Westh; Daniel E Otzen

doi:10.1016/j.febslet.2010.01.002

The role of protonation in protein fibrillation

Martin D Jeppesen, Peter Westh, Daniel E Otzen

Institut for Kemi - Center for Uopløselige Proteinstrukturer

Publikation: Bidrag til tidsskrift/Konferencebidrag i tidsskrift /Bidrag til avis › Tidsskriftartikel › Forskning › peer review

26 Citationer (Scopus)

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 pK(a) values change dramatically in the fibrillar state.

Originalsprog	Engelsk
Tidsskrift	FEBS Letters
Vol/bind	584
Nummer	4
Sider (fra-til)	780-4
Antal sider	5
DOI	https://doi.org/10.1016/j.febslet.2010.01.002
Status	Udgivet - 19 feb. 2010

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10.1016/j.febslet.2010.01.002

Citationsformater

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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 pK(a) values change dramatically in the fibrillar state.",

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

author = "Jeppesen, {Martin D} and Peter Westh and Otzen, {Daniel E}",

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T1 - The role of protonation in protein fibrillation

AU - Jeppesen, Martin D

AU - Westh, Peter

AU - Otzen, Daniel E

PY - 2010/2/19

Y1 - 2010/2/19

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 pK(a) 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 pK(a) values change dramatically in the fibrillar state.

KW - Buffers

KW - Calorimetry

KW - Circular Dichroism

KW - Glucagon

KW - Hydrogen-Ion Concentration

KW - Kinetics

KW - Microscopy, Atomic Force

KW - Models, Chemical

KW - Muramidase

KW - Protein Folding

KW - Proteins

KW - Protons

KW - Thermodynamics

KW - Titrimetry

U2 - 10.1016/j.febslet.2010.01.002

DO - 10.1016/j.febslet.2010.01.002

M3 - Journal article

C2 - 20067793

SN - 1873-3468

VL - 584

SP - 780

EP - 784

JO - FEBS Letters

JF - FEBS Letters

IS - 4

ER -

The role of protonation in protein fibrillation

Abstract

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