Directed evolution of a picomolar-affinity, high-specificity antibody targeting phosphorylated tau.

ABSTRACT: Antibodies are essential biochemical reagents for detecting protein post-translational modifications (PTMs) in complex samples. However, recent efforts in developing PTM-targeting antibodies have reported frequent nonspecific binding and limited affinity of such antibodies. To address these challenges, we investigated whether directed evolution could be applied to improve the affinity of a high-specificity antibody targeting phosphothreonine 231 (pThr-231) of the human microtubule-associated protein tau. On the basis of existing structural information, we hypothesized that improving antibody affinity may come at the cost of loss in specificity. To test this hypothesis, we developed a novel approach using yeast surface display to quantify the specificity of PTM-targeting antibodies. When we

SUBMITTER: Li D 

PROVIDER: S-EPMC6078456 | biostudies-literature | 2018 Aug

REPOSITORIES: biostudies-literature