Literature DB >> 35951297

Characterization of Bacterial Amyloids by Nano-infrared Spectroscopy.

Vincent Raussens1, Jehan Waeytens2,3.   

Abstract

Atomic force microscopy has been used for decades to study the topography of proteins during aggregation but with a lack of information on the secondary structure. On the contrary, infrared spectroscopy was able to study structural changes during the aggregation, but this analysis is complicated due to the presence of different species in mixtures and the poor spatial (~μm) resolution of the FTIR microscopy. Recently, Professor Alexandre Dazzi combined those techniques in the so-called AFM-IR. This method allows acquiring IR spectra at the nanometric scale and becomes a new standard method for the characterization of amyloid fibrils and, more generally, for the aggregation of proteins.
© 2022. The Author(s), under exclusive license to Springer Science+Business Media, LLC, part of Springer Nature.

Entities:  

Keywords:  Amyloid; Atomic force microscopy; Infrared; Nanospectroscopy; Oligomers

Mesh:

Substances:

Year:  2022        PMID: 35951297     DOI: 10.1007/978-1-0716-2529-3_9

Source DB:  PubMed          Journal:  Methods Mol Biol        ISSN: 1064-3745


  20 in total

1.  Correlative infrared nanospectroscopy and transmission electron microscopy to investigate nanometric amyloid fibrils: prospects and challenges.

Authors:  David Partouche; Jérémie Mathurin; Antoine Malabirade; Sergio Marco; Christophe Sandt; Véronique Arluison; Ariane Deniset-Besseau; Sylvain Trépout
Journal:  J Microsc       Date:  2019-01-16       Impact factor: 1.758

2.  A critical concentration of N-terminal pyroglutamylated amyloid beta drives the misfolding of Ab1-42 into more toxic aggregates.

Authors:  Denise Galante; Francesco Simone Ruggeri; Giovanni Dietler; Francesca Pellistri; Elena Gatta; Alessandro Corsaro; Tullio Florio; Angelo Perico; Cristina D'Arrigo
Journal:  Int J Biochem Cell Biol       Date:  2016-08-31       Impact factor: 5.085

3.  AFM-IR: Technology and Applications in Nanoscale Infrared Spectroscopy and Chemical Imaging.

Authors:  Alexandre Dazzi; Craig B Prater
Journal:  Chem Rev       Date:  2016-12-13       Impact factor: 60.622

Review 4.  Hfq and its constellation of RNA.

Authors:  Jörg Vogel; Ben F Luisi
Journal:  Nat Rev Microbiol       Date:  2011-08-15       Impact factor: 60.633

5.  Compaction and condensation of DNA mediated by the C-terminal domain of Hfq.

Authors:  Antoine Malabirade; Kai Jiang; Krzysztof Kubiak; Alvaro Diaz-Mendoza; Fan Liu; Jeroen A van Kan; Jean-François Berret; Véronique Arluison; Johan R C van der Maarel
Journal:  Nucleic Acids Res       Date:  2017-07-07       Impact factor: 16.971

6.  Sm-like proteins in Eubacteria: the crystal structure of the Hfq protein from Escherichia coli.

Authors:  Claude Sauter; Jérôme Basquin; Dietrich Suck
Journal:  Nucleic Acids Res       Date:  2003-07-15       Impact factor: 16.971

7.  Sm and Sm-like proteins belong to a large family: identification of proteins of the U6 as well as the U1, U2, U4 and U5 snRNPs.

Authors:  B Séraphin
Journal:  EMBO J       Date:  1995-05-01       Impact factor: 11.598

8.  New insight into the structure and function of Hfq C-terminus.

Authors:  Emilie Fortas; Federica Piccirilli; Antoine Malabirade; Valeria Militello; Sylvain Trépout; Sergio Marco; Aziz Taghbalout; Véronique Arluison
Journal:  Biosci Rep       Date:  2015-04-28       Impact factor: 3.840

9.  Infrared nanospectroscopy characterization of oligomeric and fibrillar aggregates during amyloid formation.

Authors:  F S Ruggeri; G Longo; S Faggiano; E Lipiec; A Pastore; G Dietler
Journal:  Nat Commun       Date:  2015-07-28       Impact factor: 14.919

Review 10.  Lsm proteins and Hfq: Life at the 3' end.

Authors:  Carol J Wilusz; Jeffrey Wilusz
Journal:  RNA Biol       Date:  2013-02-07       Impact factor: 4.652

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