Article ID | Journal | Published Year | Pages | File Type |
---|---|---|---|---|
2487635 | Journal of Pharmaceutical Sciences | 2007 | 16 Pages |
Abstract
Gelatin prepared from animal sources is widely used as a stabilizer in vaccine formulations. The disadvantages associated with their use such as heterogeneity and allerginicity, have led to the development of recombinant human gelatins (rhGs) as a substitute. This study focuses on characterizing the structure and monitoring the physical stability of four molecular weights (â¼8.5, 25, 50, and 100Â kDa) of rhGs as a function of temperature and pH. The information supplied should be useful in predicting the behavior of rhGs under formulation conditions. A number of spectroscopic techniques were employed in this study. Experimental results indicated that the solution properties of all four rhGs were unpredictable with microâaggregation observed at various pH values. The 8.5Â kDa rhG was found to be in a microâaggregated state at pH 5 while the 25Â kDa rhG was found to be more aggregated at pHs 5, 7, and 8. The properties of these aggregates have been analyzed as a function of temperature. The rhGs were also found to complex with the polyanion heparin through electrostatic and nonelectrostatic interactions. The stability of these complexes has been studied as a function of temperature and pH. © 2007 WileyâLiss, Inc. and the American Pharmacists Association J Pharm Sci 96: 3363-3378, 2007
Keywords
Related Topics
Health Sciences
Pharmacology, Toxicology and Pharmaceutical Science
Drug Discovery
Authors
Nagarajan Thyagarajapuram, David Olsen, C.Russell Middaugh,