ArticlemAbs2025
Enhanced rational protein engineering to reduce viscosity in high-concentration IgG1 antibody solutions.
Article in mAbs, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 1 paper.
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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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Who cites it
1 citing paper in PubMed.
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Authors and funding
7 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Subcutaneous (SC) delivery of therapeutic antibodies can offer multiple benefits to patients and healthcare providers, including convenience, time savings, and cost reduction. To improve the SC injection experience, drug developers may seek a low injection volume (1-2 mL), which for some antibody drugs necessitates a high concentration solution (≥100 mg/mL) to meet dosage requirements. Several molecular-level challenges hinder the development of high concentration antibody drug products, including high viscosity caused by reversible self-association (RSA). Here, we take an enhanced rational design approach to reduce RSA via protein engineering. Using hydrogen-deuterium exchange mass spectrometry (HDX-MS), we identified potential self-interaction hotspots on the surface of an in-house IgG1 which has known viscosity issues at high concentration. Then, using
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Registered trials
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