4.7 Article Proceedings Paper

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

期刊

JOURNAL OF MOLECULAR LIQUIDS
卷 309, 期 -, 页码 -

出版社

ELSEVIER
DOI: 10.1016/j.molliq.2020.113065

关键词

BSA; Gold; pH; Reversibility; SAXS

资金

  1. Hungarian Ministry for Innovation and Technology
  2. National Research, Development and Innovation Office [NKFIH-1157-8/g2019-DT]
  3. National Research, Development and Innovation Fund of Hungary under the 2018-1.2.1-NKP funding scheme [2018-1.2.1-NKP-2018-00005]
  4. European Regional Development Fund [ITMS2014+ 313011T583]
  5. Independent Research Fund Denmark [4002-00479, 8021-00133B, 4184-00218]

向作者/读者索取更多资源

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-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. (C) 2020 The Authors. Published by Elsevier B.V.

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