Native mass spectrometry for the design and selection of protein bioreceptors for perfluorinated compounds. Issue 6 (4th February 2021)
- Record Type:
- Journal Article
- Title:
- Native mass spectrometry for the design and selection of protein bioreceptors for perfluorinated compounds. Issue 6 (4th February 2021)
- Main Title:
- Native mass spectrometry for the design and selection of protein bioreceptors for perfluorinated compounds
- Authors:
- Daems, Elise
Moro, Giulia
Berghmans, Herald
Moretto, Ligia M.
Dewilde, Silvia
Angelini, Alessandro
Sobott, Frank
De Wael, Karolien - Abstract:
- Abstract : Native mass spectrometry allows the screening of possible protein bioreceptors for perfluorinated alkyl substances. Abstract : 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.Abstract : Native mass spectrometry allows the screening of possible protein bioreceptors for perfluorinated alkyl substances. Abstract : 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. … (more)
- Is Part Of:
- Analyst. Volume 146:Issue 6(2021)
- Journal:
- Analyst
- Issue:
- Volume 146:Issue 6(2021)
- Issue Display:
- Volume 146, Issue 6 (2021)
- Year:
- 2021
- Volume:
- 146
- Issue:
- 6
- Issue Sort Value:
- 2021-0146-0006-0000
- Page Start:
- 2065
- Page End:
- 2073
- Publication Date:
- 2021-02-04
- Subjects:
- Chemistry, Analytic -- Periodicals
543 - Journal URLs:
- http://pubs.rsc.org/en/journals/journalissues/an?e=1#!issueid=an139020&type=current&issnprint=0003-2654 ↗
http://www.rsc.org/ ↗ - DOI:
- 10.1039/d0an02005b ↗
- Languages:
- English
- ISSNs:
- 0003-2654
- Deposit Type:
- Legaldeposit
- View Content:
- Available online (eLD content is only available in our Reading Rooms) ↗
- Physical Locations:
- British Library DSC - 0893.000000
British Library DSC - BLDSS-3PM
British Library STI - ELD Digital store - Ingest File:
- 16008.xml