Anions in electrothermal supercharging of proteins with electrospray ionization follow a reverse Hofmeister series.

Anions in electrothermal supercharging of proteins with electrospray ionization follow a reverse Hofmeister series.
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DOI:
10.1021/ac403398j
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发表时间:
2014-02-04
影响因子:
7.4
通讯作者:
Williams, Evan R.
Williams, Evan R.
中科院分区:
化学1区
文献类型:
--
作者:
Cassou, Catherine A.;Williams, Evan R.

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The effects of different anions on the extent of electrothermal supercharging of proteins from aqueous ammonium and sodium salt solutions were investigated. Sulfate and hydrogen phosphate are the most effective anions at producing high charge state protein ions from buffered aqueous solution, whereas iodide and perchlorate are ineffective with electrothermal supercharging. The propensity for these anions to produce high charge state protein ions follows the following trend: sulfate > hydrogen phosphate > thiocyanate > bicarbonate > chloride > formate ≈ bromide > acetate > iodide > perchlorate. This trend correlates with the reverse Hofmeister series over a wide range of salt concentrations (1 mM to 2 M) and with several physical properties, including solvent surface tension, anion viscosity B-coefficient, and anion surface/bulk partitioning coefficient, all of which are related to the Hofmeister series. The effectiveness of electrothermal supercharging does not depend on bubble formation, either from thermal degradation of the buffer or from coalescence of dissolved gas. These results provide evidence that the effect of different ions in the formation of high charge state ions by electrothermal supercharging is largely a result of Hofmeister effects on protein stability leading to protein unfolding in the heated ESI droplet.
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