We investigated the interaction of 1,2-dipalmitoyl-sn-glycero-3-phosphocholine (DPPC) lipid nanoparticles (LN) with two recombinant human serum albumins (rHSA). We demonstrate that rHSA expressed in Oryza sativia (OsrHSA) has improved secondary structure thermal stability as measured by far U/V CD spectropolarimetry (57.6+/-2.1% alpha helix,70�C) compared to rHSA expressed in Pichia  pastoris (PprHSA) (51.3+/-0.6% alpha helix,70�C). OsrHSA compared to PprHSA displayed a 7nm blue shift in intrinsic tryptophan fluorescence and an increased number of glycated sites identified by tandem mass spectrometry. Similar stability results were observed with bovine serum albumin (48.8+/-0.5% alpha helix,70�C) and defatted bovine serum albumin (43.7+/-3.2% alpha helix,70�C) suggesting the presence of fatty acids may be responsible for the improved stability of OsrHSA. Addition of DPPC LN reduced the stability of OsrHSA (50.5+/-1.0% alpha helix,70�C), but not that of PprHSA (51.8+/-0.8% apha helix,70�C). DPPC LN may disrupt stabilizing native fatty acids or interact differently with the glycated residues on OsrHSA.

Investigation of the differences in thermal stability of two recombinant human serum albumins with 1,2-dipalmitoyl-<i>sn</i>-glycero-3-phosphocholine lipid nanoparticles by U/V circular dichroism spectropolarimetry

243rd National Meeting (2012)

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Investigation of the differences in thermal stability of two recombinant human serum albumins with 1,2-dipalmitoyl-sn-glycero-3-phosphocholine lipid nanoparticles by U/V circular dichroism spectropolarimetry