DOR BioPharma says it has made advancements in the long-term stability and optimization of the formulation of RiVax, a vaccine that contains a recombinant subunit of the A chain of ricin toxin and has been shown to induce ricin-neutralizing antibodies in humans and animals. An article characterizing the conditions for maintaining long-term stability of RiVax has been published on-line in advance of print publication in the Journal of Pharmaceutical Science.
This describes optimizing conditions for maintaining the natural structure of the RiVax subunit. These conditions were established using high-throughput spectral techniques developed in the laboratory of Russell Middaugh in the Department of Pharmaceutical Chemistry at the University of Kansas, USA.
The article further describes the use of compounds that are added to solutions of protein to stabilize the structure. These essentially prevent the protein unfolding during stress conditions, such as heat, and keep it in its natural state. These studies also identified conditions to optimize the interaction of the protein with adjuvants containing aluminum salts, which are immune-enhancing agents with a long history of use in human vaccines licensed by the US Food and Drug Administration.
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