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• W2083764503 abstract "Many factors contribute to successful tumor targeting by antibodies. Besides properties of the tumor tissue and general antibody pharmacology, a relationship exists between an antibody and its antigen that can shape penetration, catabolism, specificity, and efficacy. The affinity and avidity of the binding interactions play critical roles in these dynamics. In this work, we review the principles that guide models predicting tumor penetration and cellular internalization while providing a critical overview of studies aimed at experimentally determining the specific role of affinity and avidity in these processes. One should gain the perspective that binding affinity can, in part, dictate the localization of antibodies in tumors, leading to high concentrations in the perivascular space or low concentrations diffused throughout the tumor. These patterns can be simply due to the diminution of available dose by binding antigen and are complicated by internalization and degradation stemming from slow rates of dissociation. As opposed to the trend of simply increasing affinity to increase efficacy, novel strategies that increase avidity and broaden specificity have made significant progress in tumor targeting." @default.
• W2083764503 created "2016-06-24" @default.
• W2083764503 creator A5036175382 @default.
• W2083764503 creator A5061278758 @default.
• W2083764503 date "2009-04-01" @default.
• W2083764503 modified "2023-09-23" @default.
• W2083764503 title "Affinity and Avidity in Antibody-Based Tumor Targeting" @default.
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• W2083764503 doi "https://doi.org/10.1089/cbr.2009.0627" @default.
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