Cell Biochemistry and Biophysics

, Volume 66, Issue 2, pp 297–307 | Cite as

Spectroscopic Determination of Lysozyme Conformational Changes in the Presence of Trehalose and Guanidine

  • Davide Barreca
  • Giuseppina Laganà
  • Silvana Ficarra
  • Giuseppe Gattuso
  • Salvatore Magazù
  • Roberto La Torre
  • Ester Tellone
  • Ersilia Bellocco
Original Paper


The bioprotective action of the disaccharide trehalose has been studied against the well-known denaturating agent, guanidine hydrochloride. The results indicated a direct influence of trehalose on both enzymatic activity and conformational changes of lysozyme, as shown by the decrease of the inactivation rate constant of about 1.48-fold and the loss of α-helix structure of lysozyme. In addition, ESI–MS hydrogen–deuterium (H/D) exchange experiments allowed us to correlate the structural and dynamic features of the protein in the presence of the two additives, highlighting as trehalose remarkably influenced this exchange by decreasing local protein environment changes and solvent accessibility to the amide peptide backbone, as further evidenced by circular dichroism and 1H NMR measurements.


Trehalose Lysozyme ESI–MS hydrogen–deuterium exchange Circular dichroism 1H NMR 


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Copyright information

© Springer Science+Business Media New York 2012

Authors and Affiliations

  • Davide Barreca
    • 1
  • Giuseppina Laganà
    • 1
  • Silvana Ficarra
    • 1
  • Giuseppe Gattuso
    • 1
  • Salvatore Magazù
    • 2
  • Roberto La Torre
    • 2
  • Ester Tellone
    • 1
  • Ersilia Bellocco
    • 1
  1. 1.Department of Organic and Biological ChemistryUniversity of MessinaMessinaItaly
  2. 2.Department of PhysicsUniversity of MessinaMessinaItaly

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