Copper induces structural changes in N-terminus of human prion protein

Bo Lu; Lili Zhao; Kefeng Qin

doi:10.1016/j.bbrc.2018.03.171

Copper induces structural changes in N-terminus of human prion protein

Biochem Biophys Res Commun. 2018 May 15;499(3):470-474. doi: 10.1016/j.bbrc.2018.03.171. Epub 2018 Apr 5.

Authors

Bo Lu¹, Lili Zhao², Kefeng Qin³

Affiliations

¹ Department of Physiology, Pre-Clinical College, Guangxi Medical University, Nanning, Guangxi 530021, PR China.
² Department of Neurology, University of Chicago, Chicago, IL 60637, USA.
³ Department of Physiology, Pre-Clinical College, Guangxi Medical University, Nanning, Guangxi 530021, PR China; Department of Neurology, University of Chicago, Chicago, IL 60637, USA. Electronic address: kqin1@neurology.bsd.uchicago.edu.

PMID: 29580990
DOI: 10.1016/j.bbrc.2018.03.171

Abstract

Copper ions reportedly bind to the cellular prion (PrP^C) and induce PrP proteinase K (PK) resistant from (PrP^res). PrP^C also plays a role in response to oxidative stress. By using purified human PrP23-98 containing octarepeats, we have found that Cu(II) induces PrP^res determined by Western blots and atomic force microscopy, and structural changes detected by hydrogen/deuterium exchange in the PrP N-terminus. Therefore, we have provided the evidence that copper ions play an important role in the change of N-terminus of human prion protein.

Keywords: Copper; N-terminus; Prion; Structure.

MeSH terms

Amino Acid Sequence
Copper / pharmacology*
Deuterium Exchange Measurement
Endopeptidase K / metabolism
Humans
Microscopy, Atomic Force
Prion Proteins / chemistry*
Protein Aggregates

Substances

Prion Proteins
Protein Aggregates
Copper
Endopeptidase K