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• W2038271624 abstract "Functionalization of monoclonal antibodies (mAbs) requires chemical derivatization and/or genetic manipulation. Inherent in these methods are challenges with protein heterogeneity, stability and solubility. Such perturbations could potentially be avoided by using a high affinity, non-covalent intermediate to bridge the desired functionality to a stable mAb. Recently, we engineered a binding site for a peptide named “meditope” within the Fab of trastuzumab. Proximity of the meditope site to that of protein L suggested an opportunity to enhance the meditope's moderate affinity. Joined by a peptide linker, the meditope-protein L construct has a KD ~ 180 pM - a 7000-fold increase in affinity. The construct is highly specific to the engineered trastuzumab, as demonstrated by flow cytometry. Moreover, the fusion of a bulky GFP to this construct did not affect the association with cell surface antigens. Collectively, these data indicate this specific, high affinity construct can be developed to rapidly add new functionality to mAbs." @default.
• W2038271624 created "2016-06-24" @default.
• W2038271624 creator A5026978349 @default.
• W2038271624 creator A5031350289 @default.
• W2038271624 creator A5042104278 @default.
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• W2038271624 date "2015-01-15" @default.
• W2038271624 modified "2023-09-27" @default.
• W2038271624 title "Development of a High Affinity, Non-covalent Biologic to Add Functionality to Fabs" @default.
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• W2038271624 doi "https://doi.org/10.1038/srep07817" @default.
• W2038271624 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/4295097" @default.
• W2038271624 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/25588710" @default.
• W2038271624 hasPublicationYear "2015" @default.
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