Pressure effects on the structure and stability of the hyperthermophilic trehalose/maltose-binding protein from Thermococcus litoralis

Stephane Marchal, Maria Staiano, Anna Marabotti, Annalisa Vitale, Antonio Varriale, Reinhard Langen, Sabato D'Auria

Research output: Contribution to journalArticle

Abstract

In this work, we investigated the effect of pressure on the structure and stability of the recombinant D-trehalose/ D-maltose-binding protein isolated from the hyperthermophilic archaeon Thermococcus litoralis (TMBP). The spectroscopic results obtained both in the absence and in the presence of maltose or trehalose revealed that the TMBP-Mal complex exhibits a larger structural stability under high pressure values than TMBP- Tre complex. In addition, the results also pointed out that pressure induces reversible denaturation transitions of the protein structure. By combining the fluorescence results obtained with 8-anilino-1-naphtalene sulfonate as extrinsic probe and the intrinsic indolic fluorescence of TMBP, it is evident that the protein structural changes above 400 MPa that involve the exposure to the solvent of a large portion of the hydrophobic protein domains are preceded by a partially unfolded protein structural state. The spectroscopic results have been interpreted and discussed by taking into account the X-ray structure of the protein and, in particular, the interactions of maltose and trehalose within the three-dimensional structure of TMBP.

Original languageEnglish
Pages (from-to)12804-12808
Number of pages5
JournalJournal of Physical Chemistry B
Volume113
Issue number38
DOIs
Publication statusPublished - Sep 24 2009

ASJC Scopus subject areas

  • Physical and Theoretical Chemistry
  • Materials Chemistry
  • Surfaces, Coatings and Films

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