| Records |
| Author |
Daems, E.; Moro, G.; Berghmans, H.; Moretto, L.M.; Dewilde, S.; Angelini, A.; Sobott, F.; De Wael, K. |
| Title |
Native mass spectrometry for the design and selection of protein bioreceptors for perfluorinated compounds |
Type |
A1 Journal article |
Year  |
2021 |
Publication |
Analyst |
Abbreviated Journal |
Analyst |
| Volume |
146 |
Issue |
6 |
Pages |
2065-2073 |
| Keywords |
A1 Journal article; AXES (Antwerp X-ray Analysis, Electrochemistry and Speciation) |
| 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. |
| Address |
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| Corporate Author |
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Thesis |
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| Publisher |
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Place of Publication |
|
Editor |
|
| Language |
|
Wos |
000631575100031 |
Publication Date |
2021-01-18 |
| Series Editor |
|
Series Title |
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Abbreviated Series Title |
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| Series Volume |
|
Series Issue |
|
Edition |
|
| ISSN |
0003-2654; 1364-5528 |
ISBN |
|
Additional Links |
UA library record; WoS full record |
| Impact Factor |
3.885 |
Times cited |
|
Open Access |
OpenAccess |
| Notes |
|
Approved |
Most recent IF: 3.885 |
| Call Number |
UA @ admin @ c:irua:177074 |
Serial |
8294 |
| Permanent link to this record |
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| Author |
Borhani, A.H.; Berghmans, H.; Trashin, S.; De Wael, K.; Fago, A.; Moens, L.; Habibi-Rezaei, M.; Dewilde, S. |
| Title |
Kinetic properties and heme pocket structure of two domains of the polymeric hemoglobin of Artemia in comparison with the native molecule |
Type |
A1 Journal article |
| Year |
2015 |
Publication |
Biochimica et biophysica acta : proteins and proteomics |
Abbreviated Journal |
Bba-Proteins Proteom |
| Volume |
1854 |
Issue |
10a |
Pages |
1307-1316 |
| Keywords |
A1 Journal article; AXES (Antwerp X-ray Analysis, Electrochemistry and Speciation) |
| Abstract |
In this project, we studied some physicochemical properties of two different globin domains of the polymeric hemoglobin of the brine shrimp Artemia salina and compared them with those of the native molecule. Two domains (AsHbC1D1 and AsHbC1D5) were cloned and expressed in BL21(DE3)pLysS strain of Escherichiacoli. The recombinant proteins as well as the native hemoglobin (AfHb) were purified from bacteria and frozen Artemia, respectively by standard chromatographic methods and assessed by SDS-PAGE. The heme environment of these proteins was studied by optical spectroscopy and ligand-binding kinetics (e.g. CO association and O2 binding affinity) were measured for the two recombinant proteins and the native hemoglobin. This indicates that the CO association rate for AsHbC1D1 is higher than that of AsHbC1D5 and AfHb, while the calculated P50 value for AsHbC1D1 is lower than that of AsHbC1D5 and AfHb. The geminate and bimolecular rebinding parameters indicate a significant difference between both domains. Moreover, EPR results showed that the heme pocket in AfHb is in a more closed conformation than the heme pocket in myoglobin. Finally, the reduction potential of − 0.13 V versus the standard hydrogen electrode was determined for AfHb by direct electrochemical measurements. It is about 0.06 V higher than the potential of the single domain AsHbC1D5. This work shows that each domain in the hemoglobin of Artemia has different characteristics of ligand binding. |
| Address |
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| Corporate Author |
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Thesis |
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| Publisher |
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Place of Publication |
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Editor |
|
| Language |
|
Wos |
000362307500008 |
Publication Date |
2015-05-22 |
| Series Editor |
|
Series Title |
|
Abbreviated Series Title |
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| Series Volume |
|
Series Issue |
|
Edition |
|
| ISSN |
1570-9639 |
ISBN |
|
Additional Links |
UA library record; WoS full record |
| Impact Factor |
2.773 |
Times cited |
|
Open Access |
|
| Notes |
; This work was supported by the general grant for visiting scholar of the Ministry of Science, Research and Technology of I. R. Iran and by the University of Antwerp. ; |
Approved |
Most recent IF: 2.773; 2015 IF: 2.747 |
| Call Number |
UA @ admin @ c:irua:125909 |
Serial |
5683 |
| Permanent link to this record |
