Native mass spectrometry for the design and selection of protein bioreceptors for perfluorinated compounds (Electronic supplementary information (ESI) available. See DOI: 10.1039/d0an02005b)

Biosensing platforms are answering the increasing demand for analytical tools for environmental monitoring of small molecules, such as per- and polyfluoroalkyl substances (PFAS). By transferring toxicological findings in bioreceptor design we can develop innovative pathways for biosensor design. Ind...

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Bibliographic Details
Published in:Analyst (London) 2021-01, Vol.146 (6), p.2065-2073
Main Authors: Daems, Elise, Moro, Giulia, Herald Berghmans, Moretto, Ligia M, Dewilde, Silvia, Angelini, Alessandro, Sobott, Frank, De Wael, Karolien
Format: Article
Language:English
Subjects:
Albumins
Biomolecules
Biosensors
Case studies
Cytochrome
Cytochromes
Environmental monitoring
Hemoglobin
Mass spectrometry
Perfluoro compounds
Perfluoroalkyl & polyfluoroalkyl substances
Perfluorooctane sulfonic acid
Proteins
Scientific imaging
Spectroscopy
Toxicology
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Summary:Biosensing platforms are answering the increasing demand for analytical tools for environmental monitoring of small molecules, such as per- and polyfluoroalkyl substances (PFAS). By transferring toxicological findings in bioreceptor design we can develop innovative pathways for biosensor design. Indeed, toxicological studies provide fundamental information about PFAS-biomolecule complexes that can help evaluate the applicability of the latter as bioreceptors. The toolbox of native mass spectrometry (MS) can support this evaluation, as shown by the two case studies reported in this work. The analysis of model proteins’ (i.e. albumin, haemoglobin, cytochrome c and neuroglobin) interactions with well-known PFAS, such as perfluorooctanoic acid (PFOA) and perfluorooctanesulfonic acid (PFOS), demonstrated the potential of this native MS screening approach. In the first case study, untreated albumin and delipidated albumin were compared in the presence and absence of PFOA confirming that the delipidation step increases albumin affinity for PFOA without affecting protein stability. In the second case study, the applicability of our methodology to identify potential bioreceptors for PFOS/PFOA was extended to other proteins. Structurally related haemoglobin and neuroglobin revealed a 1 : 1 complex, whereas no binding was observed for cytochrome c. These studies have value as a proof-of-concept for a general application of native MS to identify bioreceptors for toxic compounds.
ISSN:0003-2654
1364-5528
DOI:10.1039/d0an02005b