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β2-Type Amyloidlike Fibrils of Poly-l-glutamic Acid Convert into Long, Highly Ordered Helices upon Dissolution in Dimethyl Sulfoxide

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cris.lastimport.scopus2024-02-12T19:53:53Z
dc.abstract.enReplacing water with dimethyl sulfoxide (DMSO) completely reshapes the free-energy landscapes of solvated proteins. In DMSO, a powerful hydrogen-bond (HB) acceptor, formation of HBs between backbone NH groups and solvent is favored over HBs involving protein's carbonyl groups. This entails a profound structural disruption of globular proteins and proteinaceous aggregates (e.g., amyloid fibrils) upon transfer to DMSO. Here, we investigate an unusual DMSO-induced conformational transition of β2-amyloid fibrils from poly-l-glutamic acid (PLGA). The infrared spectra of β2-PLGA dissolved in DMSO lack the typical features associated with disordered conformation that are observed when amyloid fibrils from other proteins are dispersed in DMSO. Instead, the frequency and unusual narrowness of the amide I band imply the presence of highly ordered helical structures, which is supported by complementary methods, including vibrational circular dichroism and Raman optical activity. We argue that the conformation most consistent with the spectroscopic data is that of a PLGA chain essentially lacking nonhelical segments such as bends that would provide DMSO acceptors with direct access to the backbone. A structural study of DMSO-dissolved β2-PLGA by synchrotron small-angle X-ray scattering reveals the presence of long uninterrupted helices lending direct support to this hypothesis. Our study highlights the dramatic effects that solvation may have on conformational transitions of large polypeptide assemblies.
dc.affiliationUniwersytet Warszawski
dc.contributor.authorŚcibisz, Grzegorz
dc.contributor.authorJohannessen, Christian
dc.contributor.authorTobias, Fernando
dc.contributor.authorWielgus-Kutrowska, Beata
dc.contributor.authorBzowska, Maria
dc.contributor.authorBerbeć, Sylwia
dc.contributor.authorDec, Robert
dc.contributor.authorDzwolak, Wojciech
dc.contributor.authorHernik-Magoń, Agnieszka
dc.contributor.authorMolodenskiy, Dmitry
dc.contributor.authorKeiderling, Timothy A.
dc.contributor.authorSvergun, Dmitri
dc.date.accessioned2024-01-26T12:28:53Z
dc.date.available2024-01-26T12:28:53Z
dc.date.issued2018
dc.description.financeNie dotyczy
dc.description.number50
dc.description.volume122
dc.identifier.doi10.1021/ACS.JPCB.8B08308
dc.identifier.issn1520-6106
dc.identifier.urihttps://repozytorium.uw.edu.pl//handle/item/126167
dc.languageeng
dc.pbn.affiliationchemical sciences
dc.relation.ispartofJournal of Physical Chemistry B
dc.relation.pages11895–11905
dc.rightsClosedAccess
dc.sciencecloudnosend
dc.titleβ2-Type Amyloidlike Fibrils of Poly-l-glutamic Acid Convert into Long, Highly Ordered Helices upon Dissolution in Dimethyl Sulfoxide
dc.typeJournalArticle
dspace.entity.typePublication