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Genetic Encoding of a Non-Canonical Amino Acid for the Generation of Antibody-Drug Conjugates Through a Fast Bioorthogonal Reaction
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Author Correction: Covalent penicillin-protein conjugates elicit anti-drug antibodies that are clonally and

Lachlan P Deimel1,2, Lucile Moynié3, Guoxuan Sun3

  • 1Sir William Dunn School of Pathology, University of Oxford, Oxford, OX1 3RE, UK. Lachlan.Deimel@path.ox.ac.uk.

Nature Communications
|September 11, 2024
PubMed
Abstract

No abstract available in PubMed .

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Antibodies, or immunoglobulins, are critical players in the immune system's arsenal against invading pathogens. Produced by B cells and plasma cells, their primary role is to detect and bind to specific antigens, molecules found on the surface of pathogens like bacteria or viruses. Beyond antigen recognition, antibodies perform several vital functions that contribute to immune defense.
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Drug binding to proteins is a complex phenomenon influenced by various drug-related factors, each playing a significant role in the interaction between drugs and proteins within the body.
One crucial factor in drug-protein binding is the drug's lipophilicity or its affinity for fat. More lipophilic drugs tend to have higher binding extents. For example, highly lipophilic drugs like cloxacillin exhibit substantial protein binding, with as much as 95% of the drug binding to proteins. In...
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