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Advancement of Fluorescent and Structural Properties of Bovine Serum Albumin-Gold Bioconjugates in Normal and Heavy Water with pH Conditioning and Ageing

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  • Bence Fehér, Eötvös Loránd Research Network, Neutron Spectroscopy Department
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  • Judith Mihály, Eötvös Loránd Research Network
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  • Attila Demeter, Eötvös Loránd Research Network
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  • László Almásy, Eötvös Loránd Research Network
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  • András Wacha, Eötvös Loránd Research Network
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  • Zoltán Varga, Eötvös Loránd Research Network
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  • Imre Varga, Eotvos Lorand University
  • ,
  • Jan Skov Pedersen
  • Attila Bóta, Eötvös Loránd Research Network

The red-emitting fluorescent properties of bovine serum albumin (BSA)–gold conjugates are commonly attributed to gold nanoclusters formed by metallic and ionized gold atoms, stabilized by the protein. Others argue that red fluorescence originates from gold cation–protein complexes instead, not gold nanoclusters. Our fluorescence and infrared spectroscopy, neutron, and X-ray small-angle scattering measurements show that the fluorescence and structural behavior of BSA–Au conjugates are different in normal and heavy water, strengthening the argument for the existence of loose ionic gold–protein complexes. The quantum yield for red-emitting luminescence is higher in heavy water (3.5%) than normal water (2.4%), emphasizing the impact of hydration effects. Changes in red luminescence are associated with the perturbations of BSA conformations and alterations to interatomic gold–sulfur and gold–oxygen interactions. The relative alignment of domains I and II, II and III, III and IV of BSA, determined from small-angle scattering measurements, indicate a loose (“expanded-like”) structure at pH 12 (pD ~12); by contrast, at pH 7 (pD ~7), a more regular formation appears with an increased distance between the I and II domains, suggesting the localization of gold atoms in these regions.

Antal sider13
StatusUdgivet - 25 jan. 2022

Bibliografisk note

Funding Information:
Funding: This research was funded by the National Research, Development and Innovation Office Hungary under grants K131657 (A. Bóta) and K131594 (J. Mihály) and also by Project no. 2018-1.2.1-NKP-2018-00005 under the 2018-1.2.1-NKP funding scheme (A. Bóta, Z. Varga).

Publisher Copyright:
© 2022 by the authors. Licensee MDPI, Basel, Switzerland.

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