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

Chorion is the major component of silkmoth eggshell. More than 95% of its d ry mass consists of the A and B families of low molecular weight structural proteins, which have remarkable mechanical and chemical properties, and pr otect the oocyte and the del eloping embryo from the environment. We presen t data from negative staining, Congo red binding, X-ray diffraction, Fourie r transform-Raman, attenuated total reflectance infrared spectroscopy and m odelling studies of a synthetic peptide analogue of a part of the central d omain of the B family of silkmoth chorion proteins, indicating that this pe ptide 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 a.,, FEBS Lett, 479 (2000) 141-145].: (C) 2001 Federation of European Biochemic al Societies, Published by Elsevier Science B.V. All rights reserved.