Premium
Amyloids protect the silkmoth oocyte and embryo
Author(s) -
Iconomidou Vassiliki A.,
Vriend Gert,
Hamodrakas Stavros J.
Publication year - 2000
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(00)01888-3
Subject(s) - oocyte , peptide , amyloid (mycology) , embryo , fibril , microbiology and biotechnology , biophysics , chemistry , negative stain , structural protein , biology , biochemistry , electron microscope , physics , optics , inorganic chemistry , gene
Chorion is the major component of silkmoth eggshell. More than 95% of its dry mass consists of proteins that have remarkable mechanical and chemical properties protecting the oocyte and the developing embryo from a wide range of environmental hazards. We present data from electron microscopy (negative staining and shadowing), X‐ray diffraction and modeling studies of synthetic peptide analogues of silkmoth chorion proteins indicating that chorion is a natural amyloid. The folding and self‐assembly models of chorion peptides strongly support the β‐sheet helix model of amyloid fibrils proposed recently by Blake and Serpell [Structure 4 (1996) 989–998].