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Sodium phosphate buffer increased the aggregation of rhIFN-α2b in the range of 1.55 to 1.8103 day−1, as determined by SDS/PAGE under reduced and nonreduced conditions. In contrast, sodium citrate buffer decreased the aggregation rate of this cytokine, as compared with those samples in sodium phosphate buffer. Results from sodium citrate-phosphate buffer were very similar to those obtained with sodium citrate solutions.
On the other hand, EDTA Na2×2H2O reduced the aggregation rate of rhIFN-α2b, showing an aggregation kinetic constant in the range of 0.52 to 0.75×103 day−1. Polysorbates 20 and 80 were less effective than the chelating agent in preventing this degradation pathway.
Additionally, metal ions (Zn2+ and Cu2+) increased the aggregation kinetic constant of rhIFN-α2b, probably through undetermined metal-catalyzing reactions.
Taken together, these data can be useful for the development of new formulations containing rhIFN-α2b as an active ingredient.