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  Aromaticity at position 39 in alpha-synuclein: A modulator of amyloid fibril assembly and membrane-bound conformations

Buratti, F. A., Boeffinger, N., Garro, H. A., Flores, J. S., Hita, F. J., do Carmo Goncalves, P., et al. (2022). Aromaticity at position 39 in alpha-synuclein: A modulator of amyloid fibril assembly and membrane-bound conformations. Protein Science, 31(7): e4360. doi:10.1002/pro.4360.

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Aromaticity at position 39 in ‐synuclein A modulator of amyloid fibril assembly and.pdf (Publisher version), 4MB
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Aromaticity at position 39 in ‐synuclein A modulator of amyloid fibril assembly and.pdf
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Buratti, Fiamma A., Author
Boeffinger, Nicola1, Author
Garro, Hugo A., Author
Flores, Jesica S., Author
Hita, Francisco J., Author
do Carmo Goncalves, Phelippe, Author
dos Reis Copello, Federico, Author
Lizarraga, Leonardo, Author
Rossetti, Giulia, Author
Carloni, Paolo, Author
Zweckstetter, Markus1, Author           
Outeiro, Tiago F., Author
Eimer, Stefan, Author
Griesinger, Christian1, Author                 
Fernandez, Claudio O., Author           
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1Department of NMR Based Structural Biology, Max Planck Institute for Multidisciplinary Sciences, Max Planck Society, ou_3350124              

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 Abstract: Recent studies revealed that molecular events related with the physiology and pathology of αS might be regulated by specific sequence motifs in the primary sequence of αS. The importance of individual residues in these motifs remains an important open avenue of investigation. In this work, we have addressed the structural details related to the amyloid fibril assembly and lipid-binding features of αS through the design of site-directed mutants at position 39 of the protein and their study by in vitro and in vivo assays. We demonstrated that aromaticity at position 39 of αS primary sequence influences strongly the aggregation properties and the membrane-bound conformations of the protein, molecular features that might have important repercussions for the function and dysfunction of αS. Considering that aggregation and membrane damage is an important driver of cellular toxicity in amyloid diseases, future work is needed to link our findings with studies based on toxicity and neuronal cell death.

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Language(s): eng - English
 Dates: 2022-06-27
 Publication Status: Published online
 Pages: -
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 Table of Contents: -
 Rev. Type: Peer
 Identifiers: DOI: 10.1002/pro.4360
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Project name : C.O.F. thanks Universidad Nacional de Rosario (UNR) and ANPCyT-FONCyT (PICT 2014-3704 and PICT 2017-4665) for financial support. C.O.F. and C.G. thank the Max Planck Society (P10390) for support. F.A.B. thanks CONICET for fellowship. TFO is supported by the Deutsche Forschungsgemeinschaft (DFG, German Research Foundation) under Germany's Excellence Strategy - EXC 2067/1- 390729940, and SFB1286 (Project B8). M.Z. was supported by the EU Horizon 2020 research and innovation program (grant agreement No. 787679) and by The Michael J. Fox Foundation for Parkinson's Research (Grant ID: MJFF-019033). Open Access funding enabled and organized by Projekt DEAL.
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Project name : EU Horizon 2020 research and innovation program
Grant ID : 787679
Funding program : Horizon 2020 (H2020)
Funding organization : European Commission (EC)

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Title: Protein Science
Source Genre: Journal
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Publ. Info: Hoboken, New Jersey, Vereinigte Staaten : Wiley
Pages: - Volume / Issue: 31 (7) Sequence Number: e4360 Start / End Page: - Identifier: ISSN: 0961-8368
CoNE: https://pure.mpg.de/cone/journals/resource/954925342760