We investigated the biophysical properties of four commercially available recombinant human serum albumins (rHSA) from different expression systems, as well as plasma derived HSA (pHSA). Their structure, stability, and drug binding properties were assessed with far U/V circular dichroism spectropolarimetry, differential scanning calorimetry and fluorescence spectroscopy. The heterogeneity of each sample was evaluated using reversed-phase HPLC and capillary electrophoresis. Post-translational modifications of the samples were identified by LC-MS and quantified using ion intensity based Progenesis LC-MS software. When compared to the four other albumin samples, rHSA expressed in Oryza sativa(OsrHSA) displayed  the greatest degree of  lysine and arginine residue hexose modification, superior thermal stability and resistance to chemical denaturation, reduced formation of amyloid fibrils at elevated temperatures and reduced binding of ASA. These pronounced differences in the biophysical properties of OsrHSA, when compared to other HSAs, may have implications for potential therapeutic applications.

Recombinant human serum albumin expressed in Oryza sativa displays higher stability, reduced drug binding, and greater heterogeneity than that expressed in Pichia pastoris or Saccharomyces cerevisiae

247th National Meeting (2014)

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