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

    Year: 2020

    Journal: Chem. Phys. Lipids, Volume 230, AUG

    Authors: Sandrino, B; Jochelavicius, K; Volpati, D; Barbosa, SC; Nobre, TM; Oliveira, ON

    Organizations: FAPESPFundacao de Amparo a Pesquisa do Estado de Sao Paulo (FAPESP) [2013/14262-7, 2014/12567-8]; INEO; CNPqConselho Nacional de Desenvolvimento Cientifico e Tecnologico (CNPQ); CAPES (Brazil)Coordenacao de Aperfeicoamento de Pessoal de Nivel Superior (CAPES)

    Keywords: Prion peptide; Langmuir films; Cell membrane models; Secondary structure

    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.
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