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(Reference retrieved automatically from Web of Science through information on FAPESP grant and its corresponding number as mentioned in the publication by the authors.)

The prion fragment PrP106-127 adopts a secondary structure typical of aggregated fibrils in langmuir monolayers of brain lipid extract

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Author(s):
Sandrino, B. [1] ; Jochelavicius, K. [1] ; Volpati, D. [1, 2] ; Barbosa, S. C. [1] ; Nobre, T. M. [1] ; Oliveira, Jr., O. N. [2]
Total Authors: 6
Affiliation:
[1] Univ Sao Paulo, Sao Carlos Inst Phys, BR-13560970 Sao Carlos, SP - Brazil
[2] Lund Univ, Div Solid State Phys & NanoLund, Box 118, SE-22100 Lund - Sweden
Total Affiliations: 2
Document type: Journal article
Source: Chemistry and Physics of Lipids; v. 230, AUG 2020.
Web of Science Citations: 0
Abstract

Understanding protein aggregation is essential to unveil molecular mechanisms associated with neurodegenerative diseases such as Alzheimer's, Huntington's and spongiform encephalopathy, particularly to determine the role of interaction with cell membranes. In this study, we employ Langmuir monolayers as cell membrane models to mimic interaction with the peptide KTNMHKHMAGAAAAGAVVGGLG - OH, a fragment from the human prion protein including residues 106 -127, believed to be involved in protein aggregation. Using in situ polarization-modulated infrared reflection adsorption spectroscopy (PM-IRRAS) for Langmuir monolayers and FTIR for solid films, we found that PrP106 -127 adopts mainly beta-sheets, random coils and beta-turns in Langmuir monolayers and in Langmuir-Blodgett (LB) and cast films. This also applies to monolayers and solid films made with PrP106 - 127 and a brain total lipid extract (BTLE). In contrast, some alpha-helices are observed in the secondary structure of PrP106-127 in monolayers, and especially in solid films, of 1,2-dioleoyl-sn-glycero-3-phosphocholine (DOPC). In summary, in a model representing brain cells (BTLE), the secondary structure of PrP106 - 127 is typical of fiber aggregates, while aggregation is unlikely if PrP106 - 127 interacts with a membrane model (DOPC) characteristic of mammalian cells. (AU)

FAPESP's process: 13/14262-7 - Nanostructured films from biologically-relevant materials
Grantee:Osvaldo Novais de Oliveira Junior
Support Opportunities: Research Projects - Thematic Grants
FAPESP's process: 14/12567-8 - Self-assembled peptide nanostructures: synthesis, characterization and interaction with model membrane systems
Grantee:Bianca Sandrino
Support Opportunities: Scholarships in Brazil - Post-Doctoral