Evaluation of Copper(2+) Affinities for the Prion Protein

R C Nadal; P Davies; D R Brown; J H Viles

doi:10.1021/bi9011397

Evaluation of Copper(2+) Affinities for the Prion Protein

R C Nadal, P Davies, D R Brown, J H Viles

Department of Life Sciences

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

40 Citations (SciVal)

Abstract

The prion protein (PrP) is a cell-surface Cu2+ binding glcoprotein which call 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
DOIs	https://doi.org/10.1021/bi9011397
Publication status	Published - Aug 2009

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10.1021/bi9011397

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abstract = "The prion protein (PrP) is a cell-surface Cu2+ binding glcoprotein which call 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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AU - Davies, P

AU - Brown, D R

AU - Viles, J H

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AB - The prion protein (PrP) is a cell-surface Cu2+ binding glcoprotein which call 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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JO - Biochemistry

JF - Biochemistry

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Evaluation of Copper(2+) Affinities for the Prion Protein

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