Conformational properties of the prion octa‐repeat and hydrophobic sequences

FEBS Letters

Smith, Corinne J³  Palmer, Mark S²  Bloomberg, Graham B³  Collinge, John²  Banfield, Beaulah A¹  Clarke, Anthony R³  Drake, Alex F¹ 

[1] EPSRC National Chiroptical Spectroscopy Service (Birkbeck College), 20 Gordon Street, London WC1H 0AJ, UK;Neurogenetics Unit, Department of Biochemistry, St Mary's Medical School, Imperial College, Norfolk Place, London W2 1PG, UK;Department of Biochemistry, School of Medical Sciences, University of Bristol, University Walk, Bristol BS8 1TD, UK

关键词: Circular dichroism;    PrPSc;    Peptide;    Fluorescence;    Scrapie;    TEA;    triethanolamine hydrochloride;    CD;    circular dichroism;    SDS;    sodium dodecyl sulphate;   

DOI  :  10.1016/S0014-5793(97)00220-2

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

We have used circular dichroism to study synthetic peptides from two important regions of the prion protein: the N-terminal octa-repeat domain and a highly conserved hydrophobic section. Our results show that the octa-repeat sequence in free solution can adopt a non-random, extended conformation with properties similar to the poly-l-proline type II left-handed helix. We also show that the conformation can be changed by temperature, organic solvents (e.g. acetonitrile) and on binding to phospholipid vesicles. We compared CD data from two peptides corresponding to the hydrophobic region between residues 106 and 136 which contained either methionine or valine at position 129. This variation represents a common polymorphism in humans which has been shown to influence predisposition towards iatrogenic and sporadic CJD. There was no detectable difference between the CD spectra of these peptides irrespective of the solvent conditions we used.

【 授权许可】

Unknown