Copper Binding to the N-Terminal Tandem Repeat Region of Mammalian and Avian Prion Protein: Structural Studies Using Synthetic Peptides

Using CD spectroscopy we have investigated the effect of Cu 2+ on the secondary structure of synthetic peptides Octa 4 and Hexa 4 corresponding to tetra-repeats of the octapeptide of mammalian PrP and the hexapeptide of chicken PrP. In addition, fluorescence spectroscopy was used to estimate the dis...

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Bibliographic Details
Published in:Biochemical and biophysical research communications 1995-09, Vol.214 (3), p.993-999
Main Authors: Hornshaw, M.P., Mcdermott, J.R., Candy, J.M., Lakey, J.H.
Format: Article
Language:English
Subjects:
Amino Acid Sequence
Animals
Binding Sites
Chickens
Circular Dichroism
Copper - metabolism
Kinetics
Mammals
Molecular Sequence Data
Peptide Fragments - chemical synthesis
Peptide Fragments - chemistry
Prions - chemistry
Prions - metabolism
Protein Conformation
Protein Structure, Secondary
Spectrometry, Fluorescence
Structure-Activity Relationship
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Summary:Using CD spectroscopy we have investigated the effect of Cu 2+ on the secondary structure of synthetic peptides Octa 4 and Hexa 4 corresponding to tetra-repeats of the octapeptide of mammalian PrP and the hexapeptide of chicken PrP. In addition, fluorescence spectroscopy was used to estimate the dissociation constants (Kd), of Cu 2+ binding by both peptides. Both peptides exhibited unusual CD spectra, complicated by the high proportion of aromatic residues, revealing little secondary structure in aqueous solution. Addition of Cu 2+ to Hexa 4 induced an increase in random coil to resemble Octa 4. The fluorescence of both peptides was quenched by Cu 2+ and this was used to calculate Kd′s of 6.7 μM for Octa 4 and 4.5 μM for Hexa 4. Other divalent cations showed lesser effects on the fluorescence of the peptides.
ISSN:0006-291X
1090-2104
DOI:10.1006/bbrc.1995.2384