The prion fragment PrP106-127 adopts a secondary structure typical of aggregated fibrils in langmuir monolayers of brain lipid extract
(2020) In Chemistry and Physics of Lipids 230.- 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 β-sheets, random coils and β-turns in Langmuir monolayers... (More)
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 β-sheets, random coils and β-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 α-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.
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- author
- Sandrino, B. ; Jochelavicius, K. ; Volpati, D. LU ; Barbosa, S. C. ; Nobre, T. M. and Oliveira, O. N.
- organization
- publishing date
- 2020-08-01
- type
- Contribution to journal
- publication status
- published
- subject
- keywords
- Cell membrane models, Langmuir films, Prion peptide, Secondary structure
- in
- Chemistry and Physics of Lipids
- volume
- 230
- article number
- 104930
- publisher
- Elsevier
- external identifiers
-
- scopus:85086019829
- pmid:32470442
- ISSN
- 0009-3084
- DOI
- 10.1016/j.chemphyslip.2020.104930
- language
- English
- LU publication?
- yes
- id
- 6ac61949-f2f1-44f0-a6a2-fae2da2c47c5
- date added to LUP
- 2020-06-21 21:21:39
- date last changed
- 2024-05-15 13:32:11
@article{6ac61949-f2f1-44f0-a6a2-fae2da2c47c5,
abstract = {{<p>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 β-sheets, random coils and β-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 α-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.</p>}},
author = {{Sandrino, B. and Jochelavicius, K. and Volpati, D. and Barbosa, S. C. and Nobre, T. M. and Oliveira, O. N.}},
issn = {{0009-3084}},
keywords = {{Cell membrane models; Langmuir films; Prion peptide; Secondary structure}},
language = {{eng}},
month = {{08}},
publisher = {{Elsevier}},
series = {{Chemistry and Physics of Lipids}},
title = {{The prion fragment PrP106-127 adopts a secondary structure typical of aggregated fibrils in langmuir monolayers of brain lipid extract}},
url = {{http://dx.doi.org/10.1016/j.chemphyslip.2020.104930}},
doi = {{10.1016/j.chemphyslip.2020.104930}},
volume = {{230}},
year = {{2020}},
}