The role of protonation in protein fibrillation

被引：22
|
作者：
Jeppesen, Martin D. [1 ,2 ]
Westh, Peter [3 ]
Otzen, Daniel E. [1 ,2 ]
机构：
[1] Univ Aarhus, Interdisciplinary Nanosci Ctr, Ctr Insoluble Prot Struct inSPIN, DK-8000 Aarhus C, Denmark
[2] Aalborg Hosp, Dept Life Sci, DK-9000 Aalborg, Denmark
[3] Roskilde Univ, Dept Life Sci & Chem, DK-4000 Roskilde, Denmark
来源：
FEBS LETTERS | 2010年 / 584卷 / 04期
关键词：
Fibrillation; Protonation; Glucagon; Enthalpy of elongation; Isothermal titration calorimetry; Enthalpy of ionization; ISOTHERMAL TITRATION CALORIMETRY; AMYLOID FIBRILS; GLUCAGON; DISSOCIATION;
D O I：
10.1016/j.febslet.2010.01.002
中图分类号：
Q5 [生物化学]; Q7 [分子生物学];
学科分类号：
071010 ; 081704 ;
摘要：
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. (C) 2010 Federation of European Biochemical Societies. Published by Elsevier B. V. All rights reserved.
引用
收藏
页码：780 / 784
页数：5
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