Isobaric Labeling Proteomics Allows a High-Throughput Investigation of Protein Corona Orientation
Metadatos
Afficher la notice complèteEditorial
Amer Chemical Soc
Date
2020-12-07Referencia bibliográfica
Liessi, N., Maragliano, L., Castagnola, V., Bramini, M., Benfenati, F., & Armirotti, A. (2020). Isobaric Labeling Proteomics Allows a High-Throughput Investigation of Protein Corona Orientation. Analytical Chemistry. [https://dx.doi.org/10.1021/acs.analchem.0c03134]
Patrocinador
European Commission 754446 881603; European Union's Horizon 2020 under the Marie SklodowskaCurie Action-COFUND Athenea3i 754446Résumé
The formation of the biomolecular corona represents a crucial factor in controlling the
biological interactions and trafficking of nanomaterials. In this context, the availability of key epitopes
exposed on the surface of the corona, and able to engage the biological machinery, is important to
define the biological fate of the material. While the full biomolecular corona composition can be
investigated by conventional bottom-up proteomics, the assessment of the spatial orientation of
proteins in the corona in a high-throughput fashion is still challenging. In this work, we show that
labeling corona proteins with isobaric tags in their native conditions and analyzing the MS/MS
spectra of tryptic peptides allow an easy and high-throughput assessment of the inner/outer
orientation of the corresponding proteins in the original corona. We put our results in the context of
what is currently known of the protein corona of graphene-based nanomaterials. Our conclusions are
in line with previous data and were confirmed by in silico calculations.