Bovine α1-acid glycoprotein, a thermostable version of its human counterpart: Insights from Fourier transform infrared spectroscopy and in silico modelling

Maurizio Baldassarre, Roberta Galeazzi, Beatrice Maggiore, Fabio Tanfani, Andrea Scirè

Research output: Contribution to journalArticle

Abstract

α1-Acid glycoprotein (AGP) is a plasma protein and a member of the acute phase response. AGP is known to bind and carry several biologically active compounds, as well as to down-modulate the immune system activities. In this work, the structure of bovine AGP has been investigated by Fourier-Transform infrared spectroscopy. A model structure has been obtained on the basis of human AGP and refined by molecular dynamics. In spite of the similar structure, bovine AGP shows an unexpectedly higher (∼20 °C) thermostability than its human counterpart. Inspection of the model structure has pointed out the presence of 12 ionic bridges and 2 sulphur-aromatic interactions, whereas only 6 ionic bridges were detected in human AGP. The high number (9) of glutamic acid residues involved in the ionic interactions might explain the significantly decreased thermostability measured at pH 5.5 (T m ∼ 71 °C) with respect to pH 7.4 (Tm ∼ 81 °C), whereas thermostability of human AGP was only slightly affected by lowering the pH. As in human AGP and several other lipocalins, a temperature-induced molten globule state has been observed in the denaturation pathway of bovine AGP.

Original languageEnglish
Pages (from-to)19-28
Number of pages10
JournalBiochimie
Volume102
Issue number1
DOIs
Publication statusPublished - 2014

Keywords

  • FT-IR spectroscopy
  • Lipocalins
  • Molecular dynamics
  • Molten globule-like state
  • Thermostability

ASJC Scopus subject areas

  • Biochemistry
  • Medicine(all)

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