ArticleAntibody therapeutics2026
Preventing physical and chemical degradation of the LABL-Fc-MOG
Article in Antibody therapeutics, 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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8 authors.
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Abstract
Background: LABL-Fc-MOG Methods: A high-throughput, multi-phase formulation strategy was implemented to improve conformational and colloidal stability. An initial Phase 1 evaluation used intrinsic fluorescence differential scanning fluorometry and polyethylene glycol (PEG) solubility assays to screen 96 formulations spanning a range of pH values, buffer systems, and excipients. Then, a Phase 2 study applied a definitive screening design to evaluate key formulation variables-including buffer type, excipients, and surfactant concentration-at reduced protein concentration in 96-well plates. A final Phase 3 study compared the lead formulation from Phase 2 with the control formulation at higher protein concentration in glass vials. Results: The Phase 1 study revealed pronounced sensitivity of LABL-Fc-MOG Conclusions: This work underscores the value of excipient selection and rational design of experiments in stabilizing complex fusion proteins. The optimized formulation provides a significantly enhanced stability profile and supports further development of LABL-Fc-MOG
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