Structural dependence of the cellular isoform of prion protein on solvent: spectroscopic characterization of an intermediate conformation.

Abstract:

:Using circular dichroism, fluorescence, and infrared spectroscopies, we studied the secondary structure of purified hamster PrP(C) in the presence of the mild, nonionic detergent octylglucoside. Under these native conditions, PrP(C) displayed an unexpectedly high beta-sheet component, intermediate between the values previously reported for PrP(Sc) and an isoform of PrP(C) isolated in a zwitterionic detergent. The structure of PrP(C) appeared to depend strongly on the detergent and/or phase. Switching from octylglucoside to zwitterion 3-14 drastically modified PrP secondary structure by increasing the alpha-helix while abolishing the beta-sheet component. In contrast, the conformation of PrP(C) in zwitterion was highly stable, since reverting to octylglucoside did not restore the original native structure. These and other results show that native PrP(C) in octylglucoside has some of the conformational characteristics that make the protein susceptible to conversion into PrP(Sc). Most importantly, this is the first study to demonstrate the intrinsic plasticity of the full-length native PrP(C) isolated from animal brains.

authors

Pergami P,Bramanti E,Ascoli GA

doi

10.1006/bbrc.1999.1430

subject

Has Abstract

pub_date

1999-11-02 00:00:00

pages

972-8

issue

3

eissn

0006-291X

issn

1090-2104

pii

S0006-291X(99)91430-4

journal_volume

264

pub_type

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