Copper-induced conformational change in a marsupial prion protein repeat peptide probed using FTIR spectroscopy

Marsia Gustiananda; Parvez I. Haris; Peter J. Milburn; Jill E. Gready

doi:10.1016/S0014-5793(01)03298-7

Copper-induced conformational change in a marsupial prion protein repeat peptide probed using FTIR spectroscopy

Marsia Gustiananda, Parvez I. Haris, Peter J. Milburn, Jill E. Gready^*

^*Corresponding author for this work

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

21 Citations (Scopus)

Abstract

We report the first Fourier transform infrared analysis of prion protein (PrP) repeats and the first study of PrP repeats of marsupial origin. Large changes in the secondary structure and an increase in hydrogen bonding within the peptide groups were evident from a red shift of the amide I band by >7 cm^-1 and an approximately five-fold reduction in amide hydrogen-deuterium exchange for peptide interacting with Cu²⁺ ions. Changes in the tertiary structure upon copper binding were also evident from the appearance of a new band at 1564 cm^-1, which arises from the ring vibration of histidine. The copper-induced conformational change is pH dependent, and occurs at pH >7.

Original language	English
Pages (from-to)	38-42
Number of pages	5
Journal	FEBS Letters
Volume	512
Issue number	1-3
DOIs	https://doi.org/10.1016/S0014-5793(01)03298-7
Publication status	Published - 13 Feb 2002

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title = "Copper-induced conformational change in a marsupial prion protein repeat peptide probed using FTIR spectroscopy",

abstract = "We report the first Fourier transform infrared analysis of prion protein (PrP) repeats and the first study of PrP repeats of marsupial origin. Large changes in the secondary structure and an increase in hydrogen bonding within the peptide groups were evident from a red shift of the amide I band by >7 cm-1 and an approximately five-fold reduction in amide hydrogen-deuterium exchange for peptide interacting with Cu2+ ions. Changes in the tertiary structure upon copper binding were also evident from the appearance of a new band at 1564 cm-1, which arises from the ring vibration of histidine. The copper-induced conformational change is pH dependent, and occurs at pH >7.",

keywords = "Copper binding, Fourier transform infrared spectroscopy, Marsupial protein, Prion protein, Repeat peptide, Secondary structure",

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TY - JOUR

T1 - Copper-induced conformational change in a marsupial prion protein repeat peptide probed using FTIR spectroscopy

AU - Gustiananda, Marsia

AU - Haris, Parvez I.

AU - Milburn, Peter J.

AU - Gready, Jill E.

PY - 2002/2/13

Y1 - 2002/2/13

N2 - We report the first Fourier transform infrared analysis of prion protein (PrP) repeats and the first study of PrP repeats of marsupial origin. Large changes in the secondary structure and an increase in hydrogen bonding within the peptide groups were evident from a red shift of the amide I band by >7 cm-1 and an approximately five-fold reduction in amide hydrogen-deuterium exchange for peptide interacting with Cu2+ ions. Changes in the tertiary structure upon copper binding were also evident from the appearance of a new band at 1564 cm-1, which arises from the ring vibration of histidine. The copper-induced conformational change is pH dependent, and occurs at pH >7.

AB - We report the first Fourier transform infrared analysis of prion protein (PrP) repeats and the first study of PrP repeats of marsupial origin. Large changes in the secondary structure and an increase in hydrogen bonding within the peptide groups were evident from a red shift of the amide I band by >7 cm-1 and an approximately five-fold reduction in amide hydrogen-deuterium exchange for peptide interacting with Cu2+ ions. Changes in the tertiary structure upon copper binding were also evident from the appearance of a new band at 1564 cm-1, which arises from the ring vibration of histidine. The copper-induced conformational change is pH dependent, and occurs at pH >7.

KW - Copper binding

KW - Fourier transform infrared spectroscopy

KW - Marsupial protein

KW - Prion protein

KW - Repeat peptide

KW - Secondary structure

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U2 - 10.1016/S0014-5793(01)03298-7

DO - 10.1016/S0014-5793(01)03298-7

M3 - Article

SN - 0014-5793

VL - 512

SP - 38

EP - 42

JO - FEBS Letters

JF - FEBS Letters

IS - 1-3

ER -

Copper-induced conformational change in a marsupial prion protein repeat peptide probed using FTIR spectroscopy

Abstract

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