Improving the developability of an anti-EphA2 single-chain variable fragment for nanoparticle targeting

MAbs. 2017 Jan;9(1):58-67. doi: 10.1080/19420862.2016.1259047. Epub 2016 Nov 17.

Abstract

Antibody-targeted nanoparticles have great promise as anti-cancer drugs; however, substantial developmental challenges of antibody modules prevent many candidates from reaching the clinic. Here, we describe a robust strategy for developing an EphA2-targeting antibody fragment for immunoliposomal drug delivery. A highly bioactive single-chain variable fragment (scFv) was engineered to overcome developmental liabilities, including low thermostability and weak binding to affinity purification resins. Improved thermostability was achieved by modifying the framework of the scFv, and complementarity-determining region (CDR)-H2 was modified to increase binding to protein A resins. The results of our engineering campaigns demonstrate that it is possible, using focused design strategies, to rapidly improve the stability and manufacturing characteristics of an antibody fragment for use as a component of a novel therapeutic construct.

Keywords: Antibody-drug conjugate; antibody engineering; antibody fragment; developability; liposome; manufacturability; protein A binding; stability.

MeSH terms

  • Animals
  • Drug Delivery Systems / methods*
  • Ephrin-A2 / immunology*
  • Humans
  • Immunoconjugates / immunology*
  • Immunoglobulin Variable Region / immunology
  • Nanoparticles*
  • Protein Engineering / methods
  • Protein Stability
  • Receptor, EphA2
  • Single-Chain Antibodies / biosynthesis
  • Single-Chain Antibodies / immunology*

Substances

  • EPHA2 protein, human
  • Ephrin-A2
  • Immunoconjugates
  • Immunoglobulin Variable Region
  • Single-Chain Antibodies
  • Receptor, EphA2