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

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  • Bence Fehér, Institute of Chemistry, Eotvos Lorand University
  • ,
  • Jeppe Lyngsø
  • ,
  • Boróka Bartók, Eotvos Lorand University
  • ,
  • Judith Mihály, Institute oF Materials and Environmental Chemistry
  • ,
  • Zoltán Varga, Institute oF Materials and Environmental Chemistry
  • ,
  • Róbert Mészáros, Eotvos Lorand University, János Selye University
  • ,
  • Jan Skov Pedersen
  • Attila Bóta, Institute oF Materials and Environmental Chemistry
  • ,
  • Imre Varga, Eotvos Lorand University, János Selye University

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 languageEnglish
Article number113065
JournalJournal of Molecular Liquids
Number of pages10
Publication statusPublished - 1 Jul 2020

    Research areas

  • BSA, Gold, pH, Reversibility, SAXS

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