scholarly journals Parallel β-Sheets and Polar Zippers in Amyloid Fibrils Formed by Residues 10−39 of the Yeast Prion Protein Ure2p

Biochemistry ◽  
2005 ◽  
Vol 44 (31) ◽  
pp. 10669-10680 ◽  
Author(s):  
Jerry C. C. Chan ◽  
Nathan A. Oyler ◽  
Wai-Ming Yau ◽  
Robert Tycko
Keyword(s):  
Prion Protein ◽  
Amyloid Fibrils ◽  
Yeast Prion ◽  
Β Sheets

scholarly journals Polymorphism of Amyloid Fibrils Formed by a Short Peptide from Yeast Prion Protein Sup35: AFM and Tip Enhanced Raman Scattering Study

2011 ◽  
Vol 100 (3) ◽  
pp. 539a ◽  
Author(s):  
Alexey V. Krasnoslobodtsev ◽  
Alexander M. Portillo ◽  
Tanja Deckert-Gaudig ◽  
Volker Deckert ◽  
Yuri L. Lyubchenko
Keyword(s):  
Raman Scattering ◽  
Prion Protein ◽  
Amyloid Fibrils ◽  
Yeast Prion ◽  
Short Peptide ◽  
Enhanced Raman Scattering ◽  
Scattering Study

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

2016 ◽  
Vol 165 ◽  
pp. 26-33 ◽  
Author(s):  
Alexey V. Krasnoslobodtsev ◽  
Tanja Deckert-Gaudig ◽  
Yuliang Zhang ◽  
Volker Deckert ◽  
Yuri L. Lyubchenko
Keyword(s):  
Raman Scattering ◽  
Prion Protein ◽  
Amyloid Fibrils ◽  
Yeast Prion ◽  
Enhanced Raman Scattering

scholarly journals Monitoring site-specific conformational changes in real-time reveals a misfolding mechanism of the prion protein

eLife ◽  
2019 ◽  
Vol 8 ◽  
Author(s):  
Ishita Sengupta ◽  
Jayant Udgaonkar
Keyword(s):  
Prion Protein ◽  
Conformational Changes ◽  
Amyloid Fibrils ◽  
Resonance Energy Transfer ◽  
Resonance Energy ◽  
Monitoring Site ◽  
Site Specific ◽  
Experimental Strategy ◽  
Β Sheets ◽  
Kinetics Of

During pathological aggregation, proteins undergo remarkable conformational re-arrangements to anomalously assemble into a heterogeneous collection of misfolded multimers, ranging from soluble oligomers to insoluble amyloid fibrils. Inspired by fluorescence resonance energy transfer (FRET) measurements of protein folding, an experimental strategy to study site-specific misfolding kinetics during aggregation, by effectively suppressing contributions from inter-molecular FRET, is described. Specifically, the kinetics of conformational changes across different secondary and tertiary structural segments of the mouse prion protein (moPrP) were monitored independently, after the monomeric units transformed into large oligomers OL, which subsequently disaggregated reversibly into small oligomers OS at pH 4. The sequence segments spanning helices α2 and α3 underwent a compaction during the formation of OL and elongation into β-sheets during the formation of OS. The β1-α1-β2 and α2-α3 subdomains were separated, and the helix α1 was unfolded to varying extents in both OL and OS.

Yeast prion protein New1 can break Sup35 amyloid fibrils into fragments in an ATP-dependent manner

2011 ◽  
Vol 16 (5) ◽  
pp. 545-556 ◽  
Author(s):  
Yuji Inoue ◽  
Shigeko Kawai-Noma ◽  
Ayumi Koike-Takeshita ◽  
Hideki Taguchi ◽  
Masasuke Yoshida
Keyword(s):  
Prion Protein ◽  
Amyloid Fibrils ◽  
Dependent Manner ◽  
Yeast Prion

scholarly journals Temperature-Dependent Structural Variability of Prion Protein Amyloid Fibrils

2021 ◽  
Vol 22 (10) ◽  
pp. 5075
Author(s):  
Mantas Ziaunys ◽  
Andrius Sakalauskas ◽  
Kamile Mikalauskaite ◽  
Ruta Snieckute ◽  
Vytautas Smirnovas
Keyword(s):  
Protein Aggregation ◽  
Prion Protein ◽  
Amyloid Fibrils ◽  
Prion Diseases ◽  
Morphological Properties ◽  
Large Sample Size ◽  
Structural Variations ◽  
Temperature Dependent ◽  
Protein Fibrils ◽  
Propagation Properties

Prion protein aggregation into amyloid fibrils is associated with the onset and progression of prion diseases—a group of neurodegenerative amyloidoses. The process of such aggregate formation is still not fully understood, especially regarding their polymorphism, an event where the same type of protein forms multiple, conformationally and morphologically distinct structures. Considering that such structural variations can greatly complicate the search for potential antiamyloid compounds, either by having specific propagation properties or stability, it is important to better understand this aggregation event. We have recently reported the ability of prion protein fibrils to obtain at least two distinct conformations under identical conditions, which raised the question if this occurrence is tied to only certain environmental conditions. In this work, we examined a large sample size of prion protein aggregation reactions under a range of temperatures and analyzed the resulting fibril dye-binding, secondary structure and morphological properties. We show that all temperature conditions lead to the formation of more than one fibril type and that this variability may depend on the state of the initial prion protein molecules.

scholarly journals 13C and 15N chemical shift assignments of mammalian Y145Stop prion protein amyloid fibrils

2016 ◽  
Vol 11 (1) ◽  
pp. 75-80 ◽  
Author(s):  
Theint Theint ◽  
Philippe S. Nadaud ◽  
Krystyna Surewicz ◽  
Witold K. Surewicz ◽  
Christopher P. Jaroniec
Keyword(s):  
Chemical Shift ◽  
Prion Protein ◽  
Amyloid Fibrils ◽  
Chemical Shift Assignments

scholarly journals The amphibian antimicrobial peptide uperin 3.5 is a cross-α/cross-β chameleon functional amyloid

2021 ◽  
Vol 118 (3) ◽  
pp. e2014442118
Author(s):  
Nir Salinas ◽  
Einav Tayeb-Fligelman ◽  
Massimo D. Sammito ◽  
Daniel Bloch ◽  
Raz Jelinek ◽  
...  
Keyword(s):  
Antimicrobial Peptide ◽  
Amyloid Fibrils ◽  
Amyloid Fibril ◽  
Membrane Damage ◽  
Fibril Formation ◽  
Regulation Mechanism ◽  
Bacterial Cells ◽  
Amyloid Fibril Formation ◽  
Β Amyloid ◽  
Β Sheets

Antimicrobial activity is being increasingly linked to amyloid fibril formation, suggesting physiological roles for some human amyloids, which have historically been viewed as strictly pathological agents. This work reports on formation of functional cross-α amyloid fibrils of the amphibian antimicrobial peptide uperin 3.5 at atomic resolution, an architecture initially discovered in the bacterial PSMα3 cytotoxin. The fibrils of uperin 3.5 and PSMα3 comprised antiparallel and parallel helical sheets, respectively, recapitulating properties of β-sheets. Uperin 3.5 demonstrated chameleon properties of a secondary structure switch, forming mostly cross-β fibrils in the absence of lipids. Uperin 3.5 helical fibril formation was largely induced by, and formed on, bacterial cells or membrane mimetics, and led to membrane damage and cell death. These findings suggest a regulation mechanism, which includes storage of inactive peptides as well as environmentally induced activation of uperin 3.5, via chameleon cross-α/β amyloid fibrils.

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