Reduced protein adsorption at solid interfaces by sugar excipients.
Sugar excipients are shown to reduce the adsorption of ribonuclease A, bovine serum albumin, and hen egg white lysozyme at the liquid-solid interface. The amount of protein adsorbed decreased as the concentration of the sugar increased. At the same sugar concentration, the ability of sugars to reduce protein adsorption followed the trend: trisaccharides > disaccharides > 6-carbon polyols > monosaccharides. This trend in adsorbed protein amounts among sugars was explained by stabilization of the protein native state in solution by the sugar excipients. The heat of solution of the amorphous saccharide was found to correlate with the amount of protein adsorbed.
Wendorf
Janet R
JR
Department of Chemical Engineering, University of California, Berkeley, California 94720-1462, USA.
Radke
Clayton J
CJ
Blanch
Harvey W
HW
D000327:Adsorption; D002241:Carbohydrates / Q000737:chemistry*; D057927:Hydrophobic and Hydrophilic Interactions; D007526:Isoelectric Point; D016014:Linear Models; D008970:Molecular Weight; D009113:Muramidase / Q000737:chemistry; D011506:Proteins / Q000737:chemistry*; D012259:Ribonuclease, Pancreatic / Q000737:chemistry; D012710:Serum Albumin, Bovine / Q000737:chemistry; D013499:Surface Properties; D013997:Time Factors
D002241:Carbohydrates; D011506:Proteins; D012710:Serum Albumin, Bovine; D012259:Ribonuclease, Pancreatic; D009113:Muramidase