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

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

Content Provider	World Health Organization (WHO)-Global Index Medicus
Author	Poniková, Slavomíra Antosová, Andrea Demjén, Erna Sedláková, Dagmar Marek, Jozef Varhac, Rastislav Gazová, Zuzana Sedlák, Erik
Description	Country affiliation: Slovakia Author Affiliation: Poniková S ( Department of Biophysics, Institute of Experimental Physics Slovak Academy of Sciences, Watsonova 47, 04001, Kosice, Slovakia.)
Abstract	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 ß-sheet. On the other hand, in the presence of both chaotropic perchlorate and kosmotropic sulfate anions, the fibrils form clusters with secondary structure of ß-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.
File Format	HTM / HTML
ISSN	09498257
Issue Number	6
Volume Number	20
e-ISSN	14321327
Journal	JBIC Journal of Biological Inorganic Chemistry
Language	English
Publisher	Springer
Publisher Date	2015-09-01
Publisher Place	Germany
Access Restriction	One Nation One Subscription (ONOS)
Subject Keyword	Discipline Biochemistry Amyloid Chemistry Anions Muramidase Animals Chickens Female Hydrogen-ion Concentration Protein Folding Protein Stability Protein Structure, Quaternary Temperature Journal Article Research Support, Non-u.s. Gov't
Content Type	Text
Resource Type	Article
Subject	Biochemistry Inorganic Chemistry

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

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

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