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Nanoscale spatial dependence of avidity in an IgG1 antibody

biorxiv. 2015; 
Agnieszka Jendroszek,   View Magnus Kjaergaard
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Recombinant Proteins As the avidity effect is mainly on the dissociation rate, we used the surface plasmon resonance technique to study the interaction as it allows accurate determination of off rates across orders of magnitude in time scale. Furthermore, low-density immobilization of the antibody on a surface prevents formation of higher order complexes, which may confound solution experiments. Initial screening of several commercial anti-His-tag antibodies suggested that THE His-antibody from Genscript performed best in terms of affinity and monodispersity.  Get A Quote

摘要

Antibodies are secreted proteins that are crucial to recognition of pathogens by the immune system and are also efficient pharmaceuticals. The affinity and specificity of target recognition can increase remarkably through avidity effects, when the antibody can bind a multivalent antigen though more than one epitope simultaneously. A key goal of antibody engineering is thus to optimize avidity, but little is known about the nanoscale spatial dependence of avidity in antibodies. Here, we develop a set of anti-parallel coiled-coils spanning from 7-20 nm and validate their structure using biophysical techniques. We use the coiled-coils to control the spacing between two epitopes, and measure how antigen spacing aff... More

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