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Aggregation Condition-Structure Relationship of Mouse Prion Protein Fibrils.

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cam.issuedOnline2021-09-06
dc.contributor.authorFridmanis, Jēkabs
dc.contributor.authorToleikis, Zigmantas
dc.contributor.authorSneideris, Tomas
dc.contributor.authorZiaunys, Mantas
dc.contributor.authorBobrovs, Raitis
dc.contributor.authorSmirnovas, Vytautas
dc.contributor.authorJaudzems, Kristaps
dc.contributor.orcidFridmanis, Jēkabs [0000-0002-0116-5208]
dc.contributor.orcidSneideris, Tomas [0000-0001-5285-871X]
dc.contributor.orcidSmirnovas, Vytautas [0000-0002-1829-5455]
dc.contributor.orcidJaudzems, Kristaps [0000-0003-3922-2447]
dc.date.accessioned2021-11-25T17:28:36Z
dc.date.available2021-11-25T17:28:36Z
dc.date.issued2021-09-06
dc.description.abstractPrion diseases are associated with conformational conversion of cellular prion protein into a misfolded pathogenic form, which resembles many properties of amyloid fibrils. The same prion protein sequence can misfold into different conformations, which are responsible for variations in prion disease phenotypes (prion strains). In this work, we use atomic force microscopy, FTIR spectroscopy and magic-angle spinning NMR to devise structural models of mouse prion protein fibrils prepared in three different denaturing conditions. We find that the fibril core region as well as the structure of its N- and C-terminal parts is almost identical between the three fibrils. In contrast, the central part differs in length of β-strands and the arrangement of charged residues. We propose that the denaturant ionic strength plays a major role in determining the structure of fibrils obtained in a particular condition by stabilizing fibril core interior-facing glutamic acid residues.
dc.format.mediumElectronic
dc.identifier.doi10.17863/CAM.78621
dc.identifier.eissn1422-0067
dc.identifier.issn1661-6596
dc.identifier.urihttps://www.repository.cam.ac.uk/handle/1810/331174
dc.languageeng
dc.language.isoeng
dc.publisherMDPI AG
dc.publisher.urlhttp://dx.doi.org/10.3390/ijms22179635
dc.rightsAttribution 4.0 International
dc.rights.urihttps://creativecommons.org/licenses/by/4.0/
dc.subjectaggregation conditions
dc.subjectamyloid
dc.subjectfibril structure
dc.subjectprion protein
dc.subjectAmino Acid Sequence
dc.subjectAmyloid
dc.subjectAnimals
dc.subjectCarbon Isotopes
dc.subjectMagnetic Resonance Spectroscopy
dc.subjectMice
dc.subjectMicroscopy, Atomic Force
dc.subjectNitrogen Isotopes
dc.subjectPrion Diseases
dc.subjectPrion Proteins
dc.subjectProtein Aggregation, Pathological
dc.subjectProtein Conformation
dc.subjectSpectroscopy, Fourier Transform Infrared
dc.subjectStructure-Activity Relationship
dc.titleAggregation Condition-Structure Relationship of Mouse Prion Protein Fibrils.
dc.typeArticle
dcterms.dateAccepted2021-09-03
prism.issueIdentifier17
prism.publicationDate2021
prism.publicationNameInt J Mol Sci
prism.volume22
rioxxterms.licenseref.startdate2021-09-06
rioxxterms.licenseref.urihttp://www.rioxx.net/licenses/all-rights-reserved
rioxxterms.typeJournal Article/Review
rioxxterms.versionVoR
rioxxterms.versionofrecord10.3390/ijms22179635

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