Engineering Chimeric Receptors To Investigate the Size- and Rigidity-Dependent Interaction of PEGylated Nanoparticles with Cells

ACS Nano. 2016 Jan 26;10(1):648-62. doi: 10.1021/acsnano.5b05661. Epub 2016 Jan 13.

Abstract

Attachment of ligands to the surface of nanoparticles (NPs) is an attractive approach to target specific cells and increase intracellular delivery of nanocargos. To expedite investigation of targeted NPs, we engineered human cancer cells to express chimeric receptors that bind polyethylene glycol (PEG) and internalize stealth NPs in a fashion similar to ligand-targeted liposomes against epidermal growth factor receptor 1 or 2 (HER1 or HER2), which are validated targets for cancer therapy. Measurement of the rate of endocytosis and lysosomal accumulation of small (80-94 nm) or large (180-220 nm) flexible liposomes or more rigid lipid-coated mesoporous silica particles in human HT29 colon cancer and SKBR3 breast cancer cells that express chimeric receptors revealed that larger and more rigid NPs were internalized more slowly than smaller and more flexible NPs. An exception is when both the small and large liposomes underwent endocytosis via HER2. HER1 mediated faster and greater uptake of NPs into cells but retained NPs less well as compared to HER2. Lysosomal accumulation of NPs internalized via HER1 was unaffected by NP rigidity but was inversely related to NP size, whereas large rigid NPs internalized by HER2 displayed increased lysosomal accumulation. Our results provide insight into the effects of NP properties on receptor-mediated endocytosis and suggest that anti-PEG chimeric receptors may help accelerate investigation of targeted stealth NPs.

Keywords: HER1; HER2; PEGylated liposomes; caveolin; clathrin-mediated endocytosis; immunoliposomes; polyethylene glycol; stealth NPs; αPEG antibody.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Caveolin 1 / genetics
  • Caveolin 1 / metabolism
  • Cell Engineering*
  • Cell Line, Tumor
  • Endocytosis / drug effects
  • ErbB Receptors / genetics*
  • ErbB Receptors / metabolism
  • Gene Expression
  • HT29 Cells
  • Humans
  • Liposomes / chemistry
  • Liposomes / pharmacology
  • Lysosomes / chemistry
  • Lysosomes / metabolism
  • Nanoparticles / chemistry*
  • Particle Size
  • Plasmids / chemistry
  • Plasmids / metabolism
  • Polyethylene Glycols / chemistry*
  • Polyethylene Glycols / metabolism
  • Protein Binding
  • Receptor, ErbB-2 / genetics*
  • Receptor, ErbB-2 / metabolism
  • Receptors, Artificial / genetics*
  • Receptors, Artificial / metabolism
  • Transduction, Genetic

Substances

  • Caveolin 1
  • Liposomes
  • Receptors, Artificial
  • Polyethylene Glycols
  • EGFR protein, human
  • ERBB2 protein, human
  • ErbB Receptors
  • Receptor, ErbB-2