Functional and Pharmacokinetic Properties of Antibody-Avidin Fusion Proteins

Seung Uon Shin, Dafang Wu, Rajeev Ramanathan, William M. Pardridge, Sherie L. Morrison

Research output: Contribution to journalArticle

36 Scopus citations

Abstract

In an attempt to produce broadly useful targeting agents, genetic engineering and expression techniques have been used to produce Ab-avidin fusion proteins. Chicken avidin has been fused to mouse-human chimeric IgG3 at the end of CH1 (CH1-Av), immediately after the hinge (H-Av), and at the end of CH3 (CH3-Av). Fusion heavy chains of the expected molecular mass were expressed, assembled with a co-expressed light chain, and secreted. The resulting molecules continued to bind Ag. They also bound biotinylated human serum albumin; CH3-Av had reduced affinity (KA = 5.13 × 109 M-1) compared with the tetrameric avidin (KA = 1 × 1015 M-1), but greater affinity than monomeric avidin (KA = 1 × 107 M-1). Importantly, the avidin-IgG fusion proteins had a longer serum t1/2 in rats than avidin. The favorable pharmacokinetic parameters suggest that these avidin fusion proteins can be used effectively to deliver biotinylated ligands such as drugs and peptides to locales expressing any Ag recognized by the associated Ab.

Original languageEnglish (US)
Pages (from-to)4797-4804
Number of pages8
JournalJournal of Immunology
Volume158
Issue number10
StatePublished - May 15 1997
Externally publishedYes

ASJC Scopus subject areas

  • Immunology and Allergy
  • Immunology

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  • Cite this

    Shin, S. U., Wu, D., Ramanathan, R., Pardridge, W. M., & Morrison, S. L. (1997). Functional and Pharmacokinetic Properties of Antibody-Avidin Fusion Proteins. Journal of Immunology, 158(10), 4797-4804.