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Contribution of Infrared Spectroscopy to the Understanding of Amyloid Protein Aggregation in Complex Systems.
Ami, Diletta; Mereghetti, Paolo; Natalello, Antonino.
Afiliación
  • Ami D; Department of Biotechnology and Biosciences, University of Milano-Bicocca, Milano, Italy.
  • Mereghetti P; Bioinformatics Consultant, Arquata Scrivia, Italy.
  • Natalello A; Department of Biotechnology and Biosciences, University of Milano-Bicocca, Milano, Italy.
Front Mol Biosci ; 9: 822852, 2022.
Article en En | MEDLINE | ID: mdl-35463965
ABSTRACT
Infrared (IR) spectroscopy is a label-free and non-invasive technique that probes the vibrational modes of molecules, thus providing a structure-specific spectrum. The development of infrared spectroscopic approaches that enable the collection of the IR spectrum from a selected sample area, from micro- to nano-scale lateral resolutions, allowed to extend their application to more complex biological systems, such as intact cells and tissues, thus exerting an enormous attraction in biology and medicine. Here, we will present recent works that illustrate in particular the applications of IR spectroscopy to the in situ characterization of the conformational properties of protein aggregates and to the investigation of the other biomolecules surrounding the amyloids. Moreover, we will discuss the potential of IR spectroscopy to the monitoring of cell perturbations induced by protein aggregates. The essential support of multivariate analyses to objectively pull out the significant and non-redundant information from the spectra of highly complex systems will be also outlined.
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Texto completo: 1 Colección: 01-internacional Base de datos: MEDLINE Idioma: En Revista: Front Mol Biosci Año: 2022 Tipo del documento: Article País de afiliación: Italia

Texto completo: 1 Colección: 01-internacional Base de datos: MEDLINE Idioma: En Revista: Front Mol Biosci Año: 2022 Tipo del documento: Article País de afiliación: Italia