ROLE OF POLYOLS AND SURFACTANTS IN LIQUID PROTEIN FORMULATIONS
Journal Title: WORLD JOURNAL PHARMACY AND PHARMACEUTICAL SCIENCE - Year 2017, Vol 6, Issue 6
Abstract
in aqueous protein formulations, increase conformational stability of proteins by size exclusion mechanism, increasing thermodynamic stability of proteins and decreasing aqueous solubility. Polyols prevent protein aggregation; if aggregation of the protein is preceded by partial folding or denaturation while aggregation of native protein conformation, might be enhanced by polyols. Non-ionic surfactants are excluded from water structure; thus, they are expected to accumulate at the globular protein surface-water interface. Non-ionic surfactants reduce aggregation by covering hydrophobic patches on the globular protein surface result in increased interaction of their hydrophilic components with water, thus they are expected to increase solubility of the globular protein. With respect to their effect on thermodynamic stability, this needs to be determined for each particular protein.
Authors and Affiliations
Dr. M. A. Qarawi
Keywords
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