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

Verfasser / Beitragende:
[Slavomíra Poniková, Andrea Antošová, Erna Demjén, Dagmar Sedláková, Jozef Marek, Rastislav Varhač, Zuzana Gažová, Erik Sedlák]
Ort, Verlag, Jahr:
2015
Enthalten in:
JBIC Journal of Biological Inorganic Chemistry, 20/6(2015-09-01), 921-933
Format:
Artikel (online)
ID: 605507074
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024 7 0 |a 10.1007/s00775-015-1276-0  |2 doi 
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245 0 0 |a Lysozyme stability and amyloid fibrillization dependence on Hofmeister anions in acidic pH  |h [Elektronische Daten]  |c [Slavomíra Poniková, Andrea Antošová, Erna Demjén, Dagmar Sedláková, Jozef Marek, Rastislav Varhač, Zuzana Gažová, Erik Sedlák] 
520 3 |a 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. 
540 |a SBIC, 2015 
690 7 |a Protein stability  |2 nationallicence 
690 7 |a Acidic protein  |2 nationallicence 
690 7 |a Hofmeister series  |2 nationallicence 
690 7 |a Fibrillization kinetics  |2 nationallicence 
700 1 |a Poniková  |D Slavomíra  |u Department of Biophysics, Institute of Experimental Physics Slovak Academy of Sciences, Watsonova 47, 04001, Košice, Slovakia  |4 aut 
700 1 |a Antošová  |D Andrea  |u Department of Biophysics, Institute of Experimental Physics Slovak Academy of Sciences, Watsonova 47, 04001, Košice, Slovakia  |4 aut 
700 1 |a Demjén  |D Erna  |u Department of Biophysics, Institute of Experimental Physics Slovak Academy of Sciences, Watsonova 47, 04001, Košice, Slovakia  |4 aut 
700 1 |a Sedláková  |D Dagmar  |u Department of Biophysics, Institute of Experimental Physics Slovak Academy of Sciences, Watsonova 47, 04001, Košice, Slovakia  |4 aut 
700 1 |a Marek  |D Jozef  |u Department of Biophysics, Institute of Experimental Physics Slovak Academy of Sciences, Watsonova 47, 04001, Košice, Slovakia  |4 aut 
700 1 |a Varhač  |D Rastislav  |u Department of Biochemistry, P.J. Šafárik University, Moyzesova 11, 04001, Košice, Slovakia  |4 aut 
700 1 |a Gažová  |D Zuzana  |u Department of Biophysics, Institute of Experimental Physics Slovak Academy of Sciences, Watsonova 47, 04001, Košice, Slovakia  |4 aut 
700 1 |a Sedlák  |D Erik  |u Department of Biochemistry, P.J. Šafárik University, Moyzesova 11, 04001, Košice, Slovakia  |4 aut 
773 0 |t JBIC Journal of Biological Inorganic Chemistry  |d Springer Berlin Heidelberg  |g 20/6(2015-09-01), 921-933  |x 0949-8257  |q 20:6<921  |1 2015  |2 20  |o 775 
856 4 0 |u https://doi.org/10.1007/s00775-015-1276-0  |q text/html  |z Onlinezugriff via DOI 
898 |a BK010053  |b XK010053  |c XK010000 
900 7 |a Metadata rights reserved  |b Springer special CC-BY-NC licence  |2 nationallicence 
908 |D 1  |a research-article  |2 jats 
949 |B NATIONALLICENCE  |F NATIONALLICENCE  |b NL-springer 
950 |B NATIONALLICENCE  |P 856  |E 40  |u https://doi.org/10.1007/s00775-015-1276-0  |q text/html  |z Onlinezugriff via DOI 
950 |B NATIONALLICENCE  |P 700  |E 1-  |a Poniková  |D Slavomíra  |u Department of Biophysics, Institute of Experimental Physics Slovak Academy of Sciences, Watsonova 47, 04001, Košice, Slovakia  |4 aut 
950 |B NATIONALLICENCE  |P 700  |E 1-  |a Antošová  |D Andrea  |u Department of Biophysics, Institute of Experimental Physics Slovak Academy of Sciences, Watsonova 47, 04001, Košice, Slovakia  |4 aut 
950 |B NATIONALLICENCE  |P 700  |E 1-  |a Demjén  |D Erna  |u Department of Biophysics, Institute of Experimental Physics Slovak Academy of Sciences, Watsonova 47, 04001, Košice, Slovakia  |4 aut 
950 |B NATIONALLICENCE  |P 700  |E 1-  |a Sedláková  |D Dagmar  |u Department of Biophysics, Institute of Experimental Physics Slovak Academy of Sciences, Watsonova 47, 04001, Košice, Slovakia  |4 aut 
950 |B NATIONALLICENCE  |P 700  |E 1-  |a Marek  |D Jozef  |u Department of Biophysics, Institute of Experimental Physics Slovak Academy of Sciences, Watsonova 47, 04001, Košice, Slovakia  |4 aut 
950 |B NATIONALLICENCE  |P 700  |E 1-  |a Varhač  |D Rastislav  |u Department of Biochemistry, P.J. Šafárik University, Moyzesova 11, 04001, Košice, Slovakia  |4 aut 
950 |B NATIONALLICENCE  |P 700  |E 1-  |a Gažová  |D Zuzana  |u Department of Biophysics, Institute of Experimental Physics Slovak Academy of Sciences, Watsonova 47, 04001, Košice, Slovakia  |4 aut 
950 |B NATIONALLICENCE  |P 700  |E 1-  |a Sedlák  |D Erik  |u Department of Biochemistry, P.J. Šafárik University, Moyzesova 11, 04001, Košice, Slovakia  |4 aut 
950 |B NATIONALLICENCE  |P 773  |E 0-  |t JBIC Journal of Biological Inorganic Chemistry  |d Springer Berlin Heidelberg  |g 20/6(2015-09-01), 921-933  |x 0949-8257  |q 20:6<921  |1 2015  |2 20  |o 775