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Reduced protein adsorption at solid interfaces by sugar excipients
Author(s) -
Wendorf Janet R.,
Radke Clayton J.,
Blanch Harvey W.
Publication year - 2004
Publication title -
biotechnology and bioengineering
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.136
H-Index - 189
eISSN - 1097-0290
pISSN - 0006-3592
DOI - 10.1002/bit.20132
Subject(s) - adsorption , sugar , chemistry , monosaccharide , bovine serum albumin , chromatography , lysozyme , sucrose , protein adsorption , organic chemistry , biochemistry
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. © 2004 Wiley Periodicals, Inc.