JBIC Journal of Biological Inorganic Chemistry

, Volume 20, Issue 6, pp 921–933 | Cite as

Lysozyme stability and amyloid fibrillization dependence on Hofmeister anions in acidic pH

  • Slavomíra Poniková
  • Andrea Antošová
  • Erna Demjén
  • Dagmar Sedláková
  • Jozef Marek
  • Rastislav Varhač
  • Zuzana GažováEmail author
  • Erik SedlákEmail author
Original Paper


We have explored an effect of Hofmeister anions, Na2SO4, NaCl, NaBr, NaNO3, NaSCN and NaClO4, on stability and amyloid fibrillization of hen egg white lysozyme at pH 2.7. The stability of the protein was analyzed by differential scanning calorimetry. The Hofmeister effect of the anions was assessed by the parameter dT trs/d[anion] (T trs, transition temperature). We show that dT trs/d[anion] correlates with anion surface tension effects and anion partition coefficients indicating direct interactions between anions and lysozyme. The kinetic of amyloid fibrillization of lysozyme was followed by Thioflavin T (ThT) fluorescence. Negative correlation between dT trs/d[anion] and the nucleation rate of fibrillization in the presence of monovalent anions indicates specific effect of anions on fibrillization rate of lysozyme. The efficiency of monovalent anions to accelerate fibrillization correlates with inverse Hofmeister series. The far-UV circular dichroism spectroscopy and atomic force microscopy findings show that conformational properties of fibrils depend on fibrillization rate. In the presence of sodium chloride, lysozyme forms typical fibrils with elongated structure and with the secondary structure of the β-sheet. On the other hand, in the presence of both chaotropic perchlorate and kosmotropic sulfate anions, the fibrils form clusters with secondary structure of β-turn. Moreover, the acceleration of fibril formation is accompanied by decreased amount of the formed fibrils as indicated by ThT fluorescence. Taken together, our study shows Hofmeister effect of monovalent anions on: (1) lysozyme stability; (2) ability to accelerate nucleation phase of lysozyme fibrillization; (3) amount, and (4) conformational properties of the formed fibrils.


Protein stability Acidic protein Hofmeister series Fibrillization kinetics 



This work was supported by research grants from the Slovak Grant Agency VEGA (Projects No. 1/0521/12, 2/0181/13, 2/0175/14), from Slovak Research and Development Agency (Project APVV 0526-11), ESF 26220220005, and from CELIM (316310) funded by 7FP EU (REGPOT). We also thank Ivana Petrenčáková for her editorial help in preparing the manuscript.

Supplementary material

775_2015_1276_MOESM1_ESM.pdf (220 kb)
Supplementary material 1 (PDF 219 kb)


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Copyright information

© SBIC 2015

Authors and Affiliations

  • Slavomíra Poniková
    • 1
  • Andrea Antošová
    • 1
  • Erna Demjén
    • 1
  • Dagmar Sedláková
    • 1
  • Jozef Marek
    • 1
  • Rastislav Varhač
    • 2
  • Zuzana Gažová
    • 1
    Email author
  • Erik Sedlák
    • 2
    • 3
    Email author
  1. 1.Department of Biophysics, Institute of Experimental Physics Slovak Academy of SciencesKošiceSlovakia
  2. 2.Department of Biochemistry, P.J. Šafárik UniversityKošiceSlovakia
  3. 3.Centre for Interdisciplinary Biosciences, P.J. Šafárik UniversityKošiceSlovakia

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