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

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Μονάδα:
Ερευνητικό υλικό ΕΚΠΑ
Τίτλος:
Amyloid-like fibrils from an 18-residue peptide analogue of a part of
the central domain of the B-family of silkmoth chorion proteins
Γλώσσες Τεκμηρίου:
Αγγλικά
Περίληψη:
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 del eloping 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 a.,, FEBS
Lett, 479 (2000) 141-145].: (C) 2001 Federation of European Biochemical
Societies, Published by Elsevier Science B.V. All rights reserved.
Έτος δημοσίευσης:
2001
Συγγραφείς:
Iconomidou, VA
Chryssikos, GD
Gionis, V
Vriend, G and
Hoenger, A
Hamodrakas, SJ
Περιοδικό:
FEBS Letters
Εκδότης:
Wiley
Τόμος:
499
Αριθμός / τεύχος:
3
Σελίδες:
268-273
Λέξεις-κλειδιά:
silkmoth chorion protein; amyloid fibril; electron microscopy; X-ray
diffraction; Fourier transform-Raman spectroscopy; attenuated total
reflectance infrared spectroscopy; modelling
Επίσημο URL (Εκδότης):
DOI:
10.1016/S0014-5793(01)02510-8
Το ψηφιακό υλικό του τεκμηρίου δεν είναι διαθέσιμο.