Amyloid‐like aggregates of a plant protein: a case of a sweet‐tasting protein, monellin

FEBS Letters

Murata, Kazuyoshi¹  Konno, Takashi²  Nagayama, Kuniaki¹ 

[1] Department of Molecular Physiology, National Institute for Physiological Sciences, Okazaki 444-8585, Japan;Center for Brain Experiment, National Institute for Physiological Sciences, Okazaki 444-8585, Japan

关键词: Monellin;    Heat denaturation;    Amyloid;    Fibrous aggregation;    Transmission electron microscopy;    Calorimetry;    CD;    circular dichroism;    TEM;    transmission electron microscopy;    NMR;    nuclear magnetic resonance;    SAXS;    solution X-ray scattering;   

DOI  :  10.1016/S0014-5793(99)00789-9

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

We report here a novel case of amyloid-like aggregation of a plant protein. A sweet-tasting protein, monellin, experiences an irreversible heat denaturation at pH 2.5 and 85°C. Addition of 100 mM NaCl couples this process with protein aggregation. The aggregates were structured as regular fibers with ∼10 nm width and capable of binding to Congo red, similarly to well-known amyloid fibrils. The amyloid-like aggregation process was also successfully monitored with a calorimetric method. This work supports the universality of the amyloid-like aggregation, not restricted to some special categories of protein.

【 授权许可】

Unknown