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• W2000262724 abstract "Using CD spectroscopy we have investigated the effect of Cu2+ on the secondary structure of synthetic peptides Octa4 and Hexa4 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 Cu2+ 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 Cu2+ to Hexa4 induced an increase in random coil to resemble Octa4. The fluorescence of both peptides was quenched by Cu2+ and this was used to calculate Kd′s of 6.7 μM for Octa4 and 4.5 μM for Hexa4. Other divalent cations showed lesser effects on the fluorescence of the peptides." @default.
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• W2000262724 date "1995-09-01" @default.
• W2000262724 modified "2023-09-28" @default.
• W2000262724 title "Copper Binding to the N-Terminal Tandem Repeat Region of Mammalian and Avian Prion Protein: Structural Studies Using Synthetic Peptides" @default.
• W2000262724 doi "https://doi.org/10.1006/bbrc.1995.2384" @default.
• W2000262724 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/7575574" @default.
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