Amyloid‐like fibrils from an 18‐residue peptide analogue of a part of the central domain of the B‐family of silkmoth chorion proteins

FEBS Letters

Iconomidou, Vassiliki A.³  Gionis, Vassilis¹  Chryssikos, Georgios D.¹  Hamodrakas, Stavros J.³  Hoenger, Andreas²  Vriend, Gert⁴ 

[1] Theoretical and Physical Chemistry Institute, National Hellenic Research Foundation, Athens 116 35, Greece;European Molecular Biology Laboratory, Meyerhofstrasse 1, Postfach 10.2209, D-69117 Heidelberg, Germany;Department of Cell Biology and Biophysics, Faculty of Biology, University of Athens, Panepistimiopolis, Athens 157 01, Greece;CMBI, KUN, Toernooiveld 1, 6525 ED Nijmegen, The Netherlands

关键词: Silkmoth chorion protein;    Amyloid fibril;    Electron microscopy;    X-ray diffraction;    Fourier transform-Raman spectroscopy;    Attenuated total reflectance infrared spectroscopy;    Modelling;   

DOI  :  10.1016/S0014-5793(01)02510-8

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

Chorion is the major component of silkmoth eggshell. More than 95% of its dry mass consists of the A and B families of low molecular weight structural proteins, which have remarkable mechanical and chemical properties, and protect the oocyte and the developing embryo from the environment. We present data from negative staining, Congo red binding, X-ray diffraction, Fourier transform-Raman, attenuated total reflectance infrared spectroscopy and modelling studies of a synthetic peptide analogue of a part of the central domain of the B family of silkmoth chorion proteins, indicating that this peptide folds and self-assembles, forming amyloid-like fibrils. These results support further our proposal, based on experimental data from a synthetic peptide analogue of the central domain of the A family of chorion proteins, that silkmoth chorion is a natural, protective amyloid [Iconomidou et al., FEBS Lett. 479 (2000) 141–145].

【 授权许可】

Unknown