In native mass spectrometry, intact protein complex ions are formed using electrospray ionization. Ideally the oligomeric distribution of the resulting gas-phase ion resembles the distribution in solution, but nonspecific aggregation can occur if multiple analytes in a single electrospray droplet condense during droplet evaporation. Most droplet size studies have used externally controlled flow rates and large internal diameter capillaries (10s-100s �m), whereas most native mass spectrometry experiments use electrokinetically controlled solution flows through smaller inner diameter capillaries. Here, we measure initial droplet size distributions produced by an electrokinetically controlled nanoelectrospray source and use Monte Carlo simulations to quantify the extent of nonspecific aggregration that is possible during desolvation. We then compare those predictions with experimental measurements of nonspecific aggregation.

Droplet sizes, electrospray currents, and nonspecific aggregation in electrokinetically controlled native nanoelectrospray ionization

248th National Meeting (2014)

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