Biophysical Society Thematic Meeting - October 25-30, 2015

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).

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