Effect of pH on the conformation of bovine serume albumin - gold bioconjugates

Bence Fehér; Jeppe Lyngsø; Boróka Bartók; Judith Mihály; Zoltán Varga; Róbert Mészáros; Jan Skov Pedersen; Attila Bóta; Imre Varga

doi:10.1016/j.molliq.2020.113065

Effect of pH on the conformation of bovine serume albumin - gold bioconjugates

Bence Fehér, Jeppe Lyngsø, Boróka Bartók, Judith Mihály, Zoltán Varga, Róbert Mészáros, Jan Skov Pedersen, Attila Bóta, Imre Varga

Research output: Contribution to journal › Article › peer-review

16 Scopus citations

Abstract

Biodegradable, biocompatible nanoparticles with tuneable fluorescence - due to their great potential in biology, medicine and sensor development - are widely studied nowadays. Recently it was shown that the complex red emitting spectroscopic feature of Bovine Serum Albumin - gold (BSA[sbnd]Au) bioconjugates can be related to the versatility of conformational changes of the BSA protein. In our study, we performed a comprehensive study on the structural changes of the host BSA molecules by infrared spectroscopy (FTIR) and small-angle X-ray scattering (SAXS). Both methods revealed that the BSA structure is not reversible after a neutral - alkali - neutral pH cycle and this behaviour is more pronounced in the presence of the gold salt (HAuCl₄). The changes in the monitored secondary structural elements of BSA-(HAuCl₄) system, with the fitted molecular shapes indicate that all steps in the synthesis route influence both the fine and the global structures of BSA and result in a complex structural prehistory dependent hindering of the total structural reversibility. A robust connection exists between the structural/conformational changes and the fluorescence behaviours.

Original language	English (US)
Article number	113065
Journal	Journal of Molecular Liquids
Volume	309
DOIs	https://doi.org/10.1016/j.molliq.2020.113065
State	Published - Jul 1 2020
Externally published	Yes

Bibliographical note

Funding Information:
This work was completed in the ELTE Thematic Excellence Programme (Synthesis+) supported by the Hungarian Ministry for Innovation and Technology as well as in the ELTE Institutional Excellence Programme supported by the National Research, Development and Innovation Office (NKFIH-1157-8/g2019-DT). Project no. 2018-1.2.1-NKP-2018-00005 has also been implemented with the support provided from the National Research, Development and Innovation Fund of Hungary, financed under the 2018-1.2.1-NKP funding scheme. This publication was produced under the operation program called Research and Innovation for the project: ?Support of research and development capacities in the area of nanochemical and supramolecular systems?, code ITMS2014+ 313011T583, funded from the resources of the European Regional Development Fund. Support from Independent Research Fund Denmark (Natural Sciences, grant no 4002-00479 and grant no 8021-00133B) and Independent Research Fund Denmark (Technology and Production, grant no 4184-00218) are gratefully acknowledged for funding.

Publisher Copyright:
© 2020 Elsevier B.V.

Keywords

BSA
Gold
Reversibility
SAXS
pH

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10.1016/j.molliq.2020.113065

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title = "Effect of pH on the conformation of bovine serume albumin - gold bioconjugates",

abstract = "Biodegradable, biocompatible nanoparticles with tuneable fluorescence - due to their great potential in biology, medicine and sensor development - are widely studied nowadays. Recently it was shown that the complex red emitting spectroscopic feature of Bovine Serum Albumin - gold (BSA[sbnd]Au) bioconjugates can be related to the versatility of conformational changes of the BSA protein. In our study, we performed a comprehensive study on the structural changes of the host BSA molecules by infrared spectroscopy (FTIR) and small-angle X-ray scattering (SAXS). Both methods revealed that the BSA structure is not reversible after a neutral - alkali - neutral pH cycle and this behaviour is more pronounced in the presence of the gold salt (HAuCl4). The changes in the monitored secondary structural elements of BSA-(HAuCl4) system, with the fitted molecular shapes indicate that all steps in the synthesis route influence both the fine and the global structures of BSA and result in a complex structural prehistory dependent hindering of the total structural reversibility. A robust connection exists between the structural/conformational changes and the fluorescence behaviours.",

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author = "Bence Feh{\'e}r and Jeppe Lyngs{\o} and Bor{\'o}ka Bart{\'o}k and Judith Mih{\'a}ly and Zolt{\'a}n Varga and R{\'o}bert M{\'e}sz{\'a}ros and Pedersen, {Jan Skov} and Attila B{\'o}ta and Imre Varga",

note = "Funding Information: This work was completed in the ELTE Thematic Excellence Programme (Synthesis+) supported by the Hungarian Ministry for Innovation and Technology as well as in the ELTE Institutional Excellence Programme supported by the National Research, Development and Innovation Office (NKFIH-1157-8/g2019-DT). Project no. 2018-1.2.1-NKP-2018-00005 has also been implemented with the support provided from the National Research, Development and Innovation Fund of Hungary, financed under the 2018-1.2.1-NKP funding scheme. This publication was produced under the operation program called Research and Innovation for the project: ?Support of research and development capacities in the area of nanochemical and supramolecular systems?, code ITMS2014+ 313011T583, funded from the resources of the European Regional Development Fund. Support from Independent Research Fund Denmark (Natural Sciences, grant no 4002-00479 and grant no 8021-00133B) and Independent Research Fund Denmark (Technology and Production, grant no 4184-00218) are gratefully acknowledged for funding. Publisher Copyright: {\textcopyright} 2020 Elsevier B.V.",

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doi = "10.1016/j.molliq.2020.113065",

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AU - Fehér, Bence

AU - Lyngsø, Jeppe

AU - Bartók, Boróka

AU - Mihály, Judith

AU - Varga, Zoltán

AU - Mészáros, Róbert

AU - Pedersen, Jan Skov

AU - Bóta, Attila

AU - Varga, Imre

N1 - Funding Information: This work was completed in the ELTE Thematic Excellence Programme (Synthesis+) supported by the Hungarian Ministry for Innovation and Technology as well as in the ELTE Institutional Excellence Programme supported by the National Research, Development and Innovation Office (NKFIH-1157-8/g2019-DT). Project no. 2018-1.2.1-NKP-2018-00005 has also been implemented with the support provided from the National Research, Development and Innovation Fund of Hungary, financed under the 2018-1.2.1-NKP funding scheme. This publication was produced under the operation program called Research and Innovation for the project: ?Support of research and development capacities in the area of nanochemical and supramolecular systems?, code ITMS2014+ 313011T583, funded from the resources of the European Regional Development Fund. Support from Independent Research Fund Denmark (Natural Sciences, grant no 4002-00479 and grant no 8021-00133B) and Independent Research Fund Denmark (Technology and Production, grant no 4184-00218) are gratefully acknowledged for funding. Publisher Copyright: © 2020 Elsevier B.V.

PY - 2020/7/1

Y1 - 2020/7/1

N2 - Biodegradable, biocompatible nanoparticles with tuneable fluorescence - due to their great potential in biology, medicine and sensor development - are widely studied nowadays. Recently it was shown that the complex red emitting spectroscopic feature of Bovine Serum Albumin - gold (BSA[sbnd]Au) bioconjugates can be related to the versatility of conformational changes of the BSA protein. In our study, we performed a comprehensive study on the structural changes of the host BSA molecules by infrared spectroscopy (FTIR) and small-angle X-ray scattering (SAXS). Both methods revealed that the BSA structure is not reversible after a neutral - alkali - neutral pH cycle and this behaviour is more pronounced in the presence of the gold salt (HAuCl4). The changes in the monitored secondary structural elements of BSA-(HAuCl4) system, with the fitted molecular shapes indicate that all steps in the synthesis route influence both the fine and the global structures of BSA and result in a complex structural prehistory dependent hindering of the total structural reversibility. A robust connection exists between the structural/conformational changes and the fluorescence behaviours.

AB - Biodegradable, biocompatible nanoparticles with tuneable fluorescence - due to their great potential in biology, medicine and sensor development - are widely studied nowadays. Recently it was shown that the complex red emitting spectroscopic feature of Bovine Serum Albumin - gold (BSA[sbnd]Au) bioconjugates can be related to the versatility of conformational changes of the BSA protein. In our study, we performed a comprehensive study on the structural changes of the host BSA molecules by infrared spectroscopy (FTIR) and small-angle X-ray scattering (SAXS). Both methods revealed that the BSA structure is not reversible after a neutral - alkali - neutral pH cycle and this behaviour is more pronounced in the presence of the gold salt (HAuCl4). The changes in the monitored secondary structural elements of BSA-(HAuCl4) system, with the fitted molecular shapes indicate that all steps in the synthesis route influence both the fine and the global structures of BSA and result in a complex structural prehistory dependent hindering of the total structural reversibility. A robust connection exists between the structural/conformational changes and the fluorescence behaviours.

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JF - Journal of Molecular Liquids

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ER -

Effect of pH on the conformation of bovine serume albumin - gold bioconjugates

Abstract

Bibliographical note

Keywords

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