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Amyloid-like fibrils from an 18-residue ... ly of silkmoth chorion proteins
Amyloid-like fibrils from an 18-residue peptide analogue of a part of the central domain of the B-family of silkmoth chorion proteins.
18
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].
Iconomidou VA, Chryssikos GD, Gionis V, Vriend G, Hoenger A, Hamodrakas SJ
FEBS letters
2001-06-22 00:00
499
3
268-73
Amyloid,Animals,Bombyx,Crystallography, X-Ray,Egg Proteins,Fourier Analysis,Models, Molecular,Peptides,Protein Conformation,Protein Structure, Tertiary,Spectrum Analysis, Raman,Amyloid,Egg Proteins,Peptides,chorion proteins
Department of Cell Biology and Biophysics, University of Athens, Greece
FEBS Lett.
0014-5793
S0014-5793(01)02510-8
548
True
11423129
