Evaluation of copper2+ affinities for the prion protein.

Rebecca C. Nadal; P Davies; David R. Brown; John H. Viles

doi:10.1021/bi9011397

Evaluation of copper2+ affinities for the prion protein.

Rebecca C. Nadal
, P Davies
, David R. Brown
, John H. Viles (Lead / Corresponding author)

Research output: Contribution to journal › Article › peer-review

40 Citations (Scopus)

Abstract

The prion protein (PrP) is a cell-surface Cu2+ binding glycoprotein which can bind six copper ions. The role of Cu2+ in PrP function, misfolding, and prion disease has generated much interest; however, the field has been hampered by a lack of consensus with regard to the affinity of Cu2+ for PrPC. Here we build on our understanding of the appearance of visible CD spectra for full-length PrP and fragments to determine the affinity of Cu2+ for four different binding modes, with dissociation constants ranging between 13 and 66 nM at pH 7.4.

Original language	English
Pages (from-to)	8929–8931
Number of pages	3
Journal	Biochemistry
Volume	48
Issue number	38
Early online date	4 Sept 2009
DOIs	https://doi.org/10.1021/bi9011397
Publication status	Published - 29 Sept 2009

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abstract = "The prion protein (PrP) is a cell-surface Cu2+ binding glycoprotein which can bind six copper ions. The role of Cu2+ in PrP function, misfolding, and prion disease has generated much interest; however, the field has been hampered by a lack of consensus with regard to the affinity of Cu2+ for PrPC. Here we build on our understanding of the appearance of visible CD spectra for full-length PrP and fragments to determine the affinity of Cu2+ for four different binding modes, with dissociation constants ranging between 13 and 66 nM at pH 7.4.",

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N2 - The prion protein (PrP) is a cell-surface Cu2+ binding glycoprotein which can bind six copper ions. The role of Cu2+ in PrP function, misfolding, and prion disease has generated much interest; however, the field has been hampered by a lack of consensus with regard to the affinity of Cu2+ for PrPC. Here we build on our understanding of the appearance of visible CD spectra for full-length PrP and fragments to determine the affinity of Cu2+ for four different binding modes, with dissociation constants ranging between 13 and 66 nM at pH 7.4.

AB - The prion protein (PrP) is a cell-surface Cu2+ binding glycoprotein which can bind six copper ions. The role of Cu2+ in PrP function, misfolding, and prion disease has generated much interest; however, the field has been hampered by a lack of consensus with regard to the affinity of Cu2+ for PrPC. Here we build on our understanding of the appearance of visible CD spectra for full-length PrP and fragments to determine the affinity of Cu2+ for four different binding modes, with dissociation constants ranging between 13 and 66 nM at pH 7.4.

UR - http://europepmc.org/abstract/med/19697960

U2 - 10.1021/bi9011397

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SP - 8929

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JO - Biochemistry

JF - Biochemistry

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Evaluation of copper2+ affinities for the prion protein.

Abstract

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