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Polymers and Self Assembly: From Biology to Nanomaterials Poster Session II
17-POS
Board 17
Hofmeister Anions Determine the Stability and Amyloid Self-Assembly of Lysozyme
Zuzana Gazova
1
, Slavomira Ponikova
1
, Andrea Antosova
1
, Erna Demjen
1
, Dagmar Sedlakova
1
,
Jozef Marek
1
, Rastislav Varhac
2
, Erik Sedlak
2,3
.
1
Institute of Experimental Physics, Slovak Academy of Sciences, Kosice, Slovakia,
2
P. J. Safarik
University, Kosice, Slovakia,
3
Centre for Interdisciplinary Biosciences, P. J. Safarik University,
Kosice, Slovakia.
Hofmeister series of ions ranks the relative influence of ions on physico-chemical behaviour of
biomacromolecules. We have explored an effect of various Hofmeister anions on stability and
amyloid self-assembly of hen egg white lysozyme in acidic pH. The kinetics of amyloid
fibrillization in the presence of anions suggest that neutralization of positive surface charge of
lysozyme due to interaction with anions accelerates lysozyme amyloid self-assembly. The
analysis of the conformational properties of formed fibrils has shown that lysozyme forms
typical elongated fibrils with high content of ß-sheet in presence of sodium chloride. 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. Our study shows
Hofmeister effect of monovalent anions on: (i) lysozyme stability, (ii) ability to accelerate
nucleation phase of lysozyme fibrillization, (iii) amount, and (iv) conformational properties of
the formed fibrils.
This work was supported by research grants VEGA 1/0521/12, 2/0181/13, 2/0175/14, APVV
0526-11 and from CELIM (316310) funded by 7FP EU (REGPOT).