Polyetheylenimine-polyplexes of Spiegelmer NOX-A50 directed against intracellular high mobility group protein A1 (HMGA1) reduce tumor growth in vivo

J Biol Chem. 2010 Dec 17;285(51):40012-8. doi: 10.1074/jbc.M110.178533. Epub 2010 Oct 20.

Abstract

High mobility group A1 (HMGA1) proteins belong to a group of architectural transcription factors that are overexpressed in a range of human malignancies, including pancreatic adenocarcinoma. They promote anchorage-independent growth and epithelial-mesenchymal transition and are therefore suggested as potential therapeutic targets. Employing in vitro selection techniques against a chosen fragment of HMGA1, we have generated biostable l-RNA oligonucleotides, so-called Spiegelmers, that specifically bind HMGA1b with low nanomolar affinity. We demonstrate that the best binding Spiegelmers, NOX-A50 and NOX-f33, compete HMGA1b from binding to its natural binding partner, AT-rich double-stranded DNA. We describe a formulation method based on polyplex formation with branched polyethylenimine for efficient delivery of polyethylene glycol-modified Spiegelmers and show improved tissue distribution and persistence in mice. In a xenograft mouse study using the pancreatic cancer cell line PSN-1, subcutaneous administration of 2 mg/kg per day NOX-A50 formulated in polyplexes showed an enhanced delivery of NOX-A50 to the tumor and a significant reduction of tumor volume. Our results demonstrate that intracellular targets can be successfully addressed with a Spiegelmer using polyethylenimine-based delivery and underline the importance of HMGA1 as a therapeutic target in pancreatic cancer.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Adenocarcinoma / drug therapy*
  • Animals
  • Aptamers, Nucleotide / pharmacology*
  • Cell Line, Tumor
  • DNA, Neoplasm / metabolism
  • Dose-Response Relationship, Drug
  • Drug Delivery Systems*
  • HMGA Proteins / antagonists & inhibitors*
  • HMGA Proteins / metabolism
  • Humans
  • Mice
  • Mice, Mutant Strains
  • Pancreatic Neoplasms / drug therapy*
  • Protein Binding
  • Xenograft Model Antitumor Assays*

Substances

  • Aptamers, Nucleotide
  • DNA, Neoplasm
  • HMGA Proteins