Records |
Author |
Moro, G.; Bottari, F.; Liberi, S.; Covaceuszach, S.; Cassetta, A.; Angelini, A.; De Wael, K.; Moretto, L.M. |
Title |
Covalent immobilization of delipidated human serum albumin on poly(pyrrole-2-carboxylic) acid film for the impedimetric detection of perfluorooctanoic acid |
Type |
A1 Journal article |
Year |
2020 |
Publication |
Bioelectrochemistry |
Abbreviated Journal |
Bioelectrochemistry |
Volume |
134 |
Issue |
|
Pages |
107540 |
Keywords |
A1 Journal article; Engineering sciences. Technology; AXES (Antwerp X-ray Analysis, Electrochemistry and Speciation) |
Abstract |
The immobilization of biomolecules at screen printed electrodes for biosensing applications is still an open challenge. To enrich the toolbox of bioelectrochemists, graphite screen printed electrodes (G-SPE) were modified with an electropolymerized film of pyrrole-2-carboxilic acid (Py-2-COOH), a pyrrole derivative rich in carboxylic acid functional groups. These functionalities are suitable for the covalent immobilization of biomolecular recognition layers. The electropolymerization was first optimized to obtain stable and conductive polymeric films, comparing two different electrolytes: sodium dodecyl sulphate (SDS) and sodium perchlorate. The G-SPE modified with Py-2-COOH in 0.1 M SDS solution showed the required properties and were further tested. A proof-of-concept study for the development of an impedimetric sensor for perfluorooctanoic acid (PFOA) was carried out using the delipidated human serum albumin (hSA) as bioreceptor. The data interpretation was supported by size exclusion chromatography and small-angle X-ray scattering (SEC-SAXS) analysis of the bioreceptor-target complex and the preliminary results suggest the possibility to further develop this biosensing strategy for toxicological and analytical studies. |
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 |
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Language |
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Wos |
000579727300004 |
Publication Date |
2020-04-27 |
Series Editor |
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Series Title |
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Abbreviated Series Title |
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Series Volume |
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Series Issue |
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Edition |
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ISSN |
1567-5394 |
ISBN |
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Additional Links |
UA library record; WoS full record; WoS citing articles |
Impact Factor |
5 |
Times cited |
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Open Access |
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Notes |
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Approved |
Most recent IF: 5; 2020 IF: 3.346 |
Call Number |
UA @ admin @ c:irua:172494 |
Serial |
6477 |
Permanent link to this record |
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Author |
Maso, L.; Trande, M.; Liberi, S.; Moro, G.; Daems, E.; Linciano, S.; Sobott, F.; Covaceuszach, S.; Cassetta, A.; Fasolato, S.; Moretto, L.M.; De Wael, K.; Cendron, L.; Angelini, A. |
Title |
Unveiling the binding mode of perfluorooctanoic acid to human serum albumin |
Type |
A1 Journal article |
Year |
2021 |
Publication |
Protein Science |
Abbreviated Journal |
Protein Sci |
Volume |
30 |
Issue |
4 |
Pages |
830-841 |
Keywords |
A1 Journal article; AXES (Antwerp X-ray Analysis, Electrochemistry and Speciation) |
Abstract |
Perfluorooctanoic acid (PFOA) is a toxic compound that is absorbed and distributed throughout the body by noncovalent binding to serum proteins such as human serum albumin (hSA). Though the interaction between PFOA and hSA has been already assessed using various analytical techniques, a high resolution and detailed analysis of the binding mode is still lacking. We report here the crystal structure of hSA in complex with PFOA and a medium-chain saturated fatty acid (FA). A total of eight distinct binding sites, four occupied by PFOAs and four by FAs, have been identified. In solution binding studies confirmed the 4:1 PFOA-hSA stoichiometry and revealed the presence of one high and three low affinity binding sites. Competition experiments with known hSA-binding drugs allowed locating the high affinity binding site in sub-domain IIIA. The elucidation of the molecular basis of the interaction between PFOA and hSA might provide not only a better assessment of the absorption and elimination mechanisms of these compounds in vivo but also have implications for the development of novel molecular receptors for diagnostic and biotechnological applications. |
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 |
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Language |
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Wos |
000625392600001 |
Publication Date |
2021-02-08 |
Series Editor |
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Series Title |
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Abbreviated Series Title |
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Series Volume |
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Series Issue |
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Edition |
|
ISSN |
0961-8368 |
ISBN |
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Additional Links |
UA library record; WoS full record; WoS citing articles |
Impact Factor |
2.523 |
Times cited |
|
Open Access |
Not_Open_Access |
Notes |
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Approved |
Most recent IF: 2.523 |
Call Number |
UA @ admin @ c:irua:176725 |
Serial |
8714 |
Permanent link to this record |