Polymorphism of amyloid fibrils formed by a peptide from the yeast prion protein Sup35: AFM and Tip-Enhanced Raman Scattering studies

Alexey V Krasnoslobodtsev, Tanja Deckert-Gaudig, Yuliang Zhang, Volker Deckert, Yuri L Lyubchenko

Research output: Contribution to journalArticle

11 Citations (Scopus)

Abstract

Aggregation of prion proteins is the cause of various prion related diseases. The infectious form of prions, amyloid aggregates, exist as multiple strains. The strains are thought to represent structurally different prion protein molecules packed into amyloid aggregates, but the knowledge on the structure of different types of aggregates is limited. Here we report on the use of AFM (Atomic Force Microscopy) and TERS (Tip-Enhanced Raman Scattering) to study morphological heterogeneity and access underlying conformational features of individual amyloid aggregates. Using AFM we identified the morphology of amyloid fibrils formed by the peptide (CGNNQQNY) from the yeast prion protein Sup35 that is critically involved in the aggregation of the full protein. TERS results demonstrate that morphologically different amyloid fibrils are composed of a distinct set of conformations. Fibrils formed at pH 5.6 are composed of a mixture of peptide conformations (β-sheets, random coil and α-helix) while fibrils formed in pH~2 solution primarily have β-sheets. Additionally, peak positions in the amide III region of the TERS spectra suggested that peptides have parallel arrangement of β-sheets for pH~2 fibrils and antiparallel arrangement for fibrils formed at pH 5.6. We also developed a methodology for detailed analysis of the peptide secondary structure by correlating intensity changes of Raman bands in different regions of TERS spectra. Such correlation established that structural composition of peptides is highly localized with large contribution of unordered secondary structures on a fibrillar surface.

Original languageEnglish (US)
Pages (from-to)26-33
Number of pages8
JournalUltramicroscopy
Volume165
DOIs
StatePublished - Jun 1 2016

Fingerprint

yeast
polymorphism
Polymorphism
Amyloid
Yeast
Peptides
peptides
Raman scattering
Atomic force microscopy
atomic force microscopy
Raman spectra
proteins
Prions
Conformations
Agglomeration
Amides
helices
amides
coils
methodology

Keywords

  • AFM
  • Aggregation
  • Amyloid
  • Prion
  • TERS

ASJC Scopus subject areas

  • Electronic, Optical and Magnetic Materials
  • Atomic and Molecular Physics, and Optics
  • Instrumentation

Cite this

Polymorphism of amyloid fibrils formed by a peptide from the yeast prion protein Sup35 : AFM and Tip-Enhanced Raman Scattering studies. / Krasnoslobodtsev, Alexey V; Deckert-Gaudig, Tanja; Zhang, Yuliang; Deckert, Volker; Lyubchenko, Yuri L.

In: Ultramicroscopy, Vol. 165, 01.06.2016, p. 26-33.

Research output: Contribution to journalArticle

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