Antimicrobial preservatives are commonly used in multi-dose protein formulations to inhibit the accidental growth of microbes and bacteria. However, these preservatives cause protein aggregation, which results in serious immunogenic and toxic effects in human patients. Regina Bis and other members from Krishna Mallela’s laboratory have recently shown that the mechanism by which antimicrobial preservatives induce protein aggregation is through partial rather than global unfolding of the protein. Stabilizing the aggregation ’hot-spot’ reduces protein aggregation. Further, various commonly used preservatives have varying effects on partial protein unfolding and aggregation. This work has been recently published in the Journal of Pharmaceutical Sciences, and was selected by the Editors to be featured on the journal’s website based on the most original and most significant scientific findings. Regina’s work is funded by the PhRMA Foundation and the National Institutes of Health Leadership Training Grant in Pharmaceutical Biotechnology. She has also been awarded a Biotechnology travel grant from the American Association of Pharmaceutical Scientists (AAPS) to present her groundbreaking results at its National Biotechnology Conference in San Diego.
Read the full article at http://onlinelibrary.wiley.com/doi/10.1002/jps.23362/full.