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

FEBS Letters

Haris, Parvez I.³  Milburn, Peter J.¹  Gustiananda, Marsia²  Gready, Jill E.² 

[1] Biomolecular Resources Facility, John Curtin School of Medical Research, Australian National University, P.O. Box 334, Canberra, ACT 2601, Australia;Computational Molecular Biology and Drug Design Group, John Curtin School of Medical Research, Australian National University, P.O. Box 334, Canberra, ACT 2601, Australia;Department of Biological Sciences, De Montfort University, The Gateway, Leicester LE1 9BH, UK

关键词: Fourier transform infrared spectroscopy;    Repeat peptide;    Prion protein;    Copper binding;    Marsupial protein;    Secondary structure;    FTIR;    Fourier transform infrared;    PrP;    prion protein;    TFA;    trifluoroacetic acid;   

DOI  :  10.1016/S0014-5793(01)03298-7

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

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.

【 授权许可】

Unknown