Site-specific antibody-polymer conjugates for siRNA delivery

J Am Chem Soc. 2013 Sep 18;135(37):13885-91. doi: 10.1021/ja4059525. Epub 2013 Sep 5.

Abstract

We describe here the development of site-specific antibody-polymer conjugates (APCs) for the selective delivery of small interference RNAs (siRNAs) to target cells. APCs were synthesized in good yields by conjugating an aminooxy-derivatized cationic block copolymer to an anti-HER2 Fab or full-length IgG by means of genetically encoded p-acetyl phenylalanine (pAcF). The APCs all showed binding affinity comparable to that of HER2 as their native counterparts and no significant cellular cytotoxicity. Mutant S202-pAcF Fab and Q389-pAcF IgG polymer conjugates specifically delivered siRNAs to HER2(+) cells and mediated potent gene silencing at both the mRNA and protein levels. However, a mutant A121-pAcF IgG polymer conjugate, despite its high binding affinity to HER2 antigen, did not induce a significant RNA interference response in HER2(+) cells, presumably due to steric interference with antigen binding and internalization. These results highlight the importance of conjugation site on the activity of antibody-polymer-based therapeutics and suggest that such chemically defined APCs may afford a useful targeted delivery platform for siRNAs or other nucleic acid-based therapies.

Publication types

  • Research Support, N.I.H., Extramural

MeSH terms

  • Antibodies / pharmacology*
  • Antibodies, Monoclonal, Humanized / pharmacology
  • Antineoplastic Agents / chemistry
  • Antineoplastic Agents / pharmacology
  • Breast Neoplasms / drug therapy
  • Cell Line, Tumor
  • Cell Survival / drug effects
  • Drug Delivery Systems*
  • Electrophoresis, Polyacrylamide Gel
  • Female
  • Humans
  • Immunoconjugates / pharmacology*
  • Microscopy, Confocal
  • Polymers / pharmacology*
  • RNA, Small Interfering / pharmacology*
  • Receptor, ErbB-2 / chemistry
  • Trastuzumab

Substances

  • Antibodies
  • Antibodies, Monoclonal, Humanized
  • Antineoplastic Agents
  • Immunoconjugates
  • Polymers
  • RNA, Small Interfering
  • ERBB2 protein, human
  • Receptor, ErbB-2
  • Trastuzumab