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- W2915002912 abstract "Protein-based ‘biologics’ — drugs derived from living organisms — are among the most effective therapeutic treatments on the market. However, biologics are unstable, have short half-lives and require low temperature storage, making them prohibitively expensive. Although some biologics can be stabilized by formulation with excipients, most still require low temperature storage. In our search for new, more robust excipients, we turned to the tardigrade, a microscopic animal that synthesizes a unique family of intrinsically disordered proteins (IDPs) that protect its cellular components during desiccation. Encapsulating a globular test protein in a tardigrade IDP hydrogel stabilizes the folded state of that protein. These tardigrade IDPs are more effective than two FDA approved excipients, trehalose and serum albumin, at protecting lactate dehydrogenase activity during desiccation. We even observe protection of lactate dehydrogenase upon heating desiccated enzyme/tardigrade IDP mixtures to 95 °C. In addition, these IDPs protect the restriction enzyme DpnI from desiccation-induced inactivation and lipoprotein lipase against both freezing-induced and lyophilization-induced inactivation. Work is underway to quantify the protection of antibodies against aggregation. In summary, we have demonstrated the ability of these tardigrade IDPs to stabilize a globular protein and protect a diverse range of enzymes against desiccation, freezing, and lyophilization." @default.
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- W2915002912 date "2019-02-01" @default.
- W2915002912 modified "2023-10-17" @default.
- W2915002912 title "Tardigrade Intrinsically Disordered Proteins Protect Enzymes from Desiccation-Induced Inactivation" @default.
- W2915002912 doi "https://doi.org/10.1016/j.bpj.2018.11.2443" @default.
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