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Amyloid‐like fibrils from an 18‐residue peptide analogue of a part of the central domain of the B‐family of silkmoth chorion proteins
Author(s) -
Iconomidou Vassiliki A.,
Chryssikos Georgios D.,
Gionis Vassilis,
Vriend Gert,
Hoenger Andreas,
Hamodrakas Stavros J.
Publication year - 2001
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/s0014-5793(01)02510-8
Subject(s) - peptide , fibril , amyloid (mycology) , chemistry , biophysics , residue (chemistry) , biochemistry , biology , inorganic chemistry
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].