The origins of nonideality exhibited by monoclonal antibodies and Fab fragments in human serum.
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ABSTRACT: The development of therapeutic antibodies remains challenging, time-consuming, and expensive. A key contributing factor is a lack of understanding of how proteins are affected by complex biological environments such as serum and plasma. Nonideality due to attractive or repulsive interactions with cosolutes can alter the stability, aggregation propensity, and binding interactions of proteins in solution. Fluorescence correlation spectroscopy (FCS) can be used to measure apparent second virial coefficient (B2,app ) values for therapeutic and model monoclonal antibodies (mAbs) that capture the nature and strength of interactions with cosolutes directly in undiluted serum and similar complex biological media. Here, we use FCS-derived B2,app measurements to identify the co
SUBMITTER: Larsen HA
PROVIDER: S-EPMC10659951 | biostudies-literature | 2023 Dec
REPOSITORIES: biostudies-literature
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