Stefanick, Jared F. published the artcileEnhancement of Antibody Selectivity via Bicyclic Complex Formation, Quality Control of 882847-32-7, the main research area is antibody antigen bicyclic complex.
This study describes a strategy where antibody selectivity for high antigen-d. surfaces is enhanced by forming a thermodynamically stable bicyclic complex. The bicyclic complex was formed via multivalent interactions of the antibody with a synthetic trivalent mimotope at a 3:2 molar ratio. Complex formation was analyzed using dynamic light scattering and anal. ultracentrifugation, showing a hydrodynamic radius of ∼22 nm and a calculated mol. weight of 397 kDa, depicting a trimeric complex formation. The complex has high thermodn. stability and results in a 10-fold higher binding affinity for the trivalent mimotope (Kd = 0.14 μM) compared to the monovalent mimotope (Kd = 1.4 μM). As bicyclic complexes, the antibodies showed ∼18% binding of the monomeric form to low antigen-d. surfaces. At high antigen-d., antibody binding was equal whether delivered as a complex or a monomer. These results establish bicyclic complex selectivity for high antigen-d. surfaces and suggest a potential method to enhance therapeutic antibody selectivity for diseased cells.
Journal of Physical Chemistry Letters published new progress about Cell. 882847-32-7 belongs to class esters-buliding-blocks, name is 1-(9H-Fluoren-9-yl)-3-oxo-2,7,10,13,16,19-hexaoxa-4-azadocosan-22-oic acid, and the molecular formula is C28H37NO9, Quality Control of 882847-32-7.
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