Discovery and optimization of a synthetic small protein domain targeting antibodies.

ABSTRACT:

Introduction

Antibodies and their derivatives constitute a crucial class of molecules in modern biotechnology and therapeutic development. Consequently, identifying chemically robust affinity ligands capable of specifically recognizing antibodies remains an important challenge.

Methods

In this study, an in-house phage display library based on the WW domain scaffold (WWp5_4) was utilized to identify binders against polyclonal human IgG. A lead ligand from clone E6 was selected. To enhance the developability of WW ligands derived from this library, we rationally minimized structural liabilities within the scaffold framework to improve chemical stability and solubility, generating two mutant variants. Furthermore, a head-to-tail dimeric version of the E6 mutant sequence was des

SUBMITTER: Dias AMGC 

PROVIDER: S-EPMC12647017 | biostudies-literature | 2025

REPOSITORIES: biostudies-literature