High stability of trehalose/maltose binding protein from Thermococcus litoralis makes it a good candidate as a sensitive element in biosensor systems for sugar control

Issue title: From Molecule to Tissue: XIII European Conference on the Spectroscopy of Biological Molecules, Palermo, Italy, August 28–September 2, 2009, Part 2 of 2

Article type: Research Article

Authors: Povarova, Olga I.^; | Stepanenko, Olga V. | Sulatskaya, Anna I. | Kuznetsova, Irina M. | Turoverov, Konstantin K. | Staiano, Maria | Vitale, Annalisa | D'Auria, Sabato

Affiliations: Institute of Cytology of the Russian Academy of Sciences, Saint-Petersburg, Russia | Institute of Protein Biochemistry CNR, Napoli, Italy

Note: [] Corresponding author: Dr. Olga I. Povarova, Scientific Associate of the Laboratory of Structural Dynamics, Stability and Protein Folding, Institute of Cytology RAS, Saint-Petersburg, Russia. Tel.: +7 812 297 19 57; Fax: +7 812 297 35 41; E-mail: olp@mail.cytspb.rssi.ru.

Abstract: Fluorescence and circular dichroism in far-UV region were used to study the stability of trehalose/maltose binding protein (TMBP) from hyper thermophilic archaeon Thermococcus litoralis and its complex with glucose (TMBP/Glc). The evaluation of difference between free energy of native and unfolded state for TMBP and TMBP/Glc showed that both of them are several times higher than that of proteins from mesophilic organisms. Due to the high stability and innate ability to bind glucose this protein is a good candidate as a sensitive element in biosensor systems for sugar control.

Keywords: Fluorescence, circular dichroism, hyperthermophilic organism, protein stability

DOI: 10.3233/SPE-2010-0469

Journal: Spectroscopy, vol. 24, no. 3-4, pp. 349-353, 2010