Elastin-like peptide amphiphiles form nanofibers with tunable length

Biomacromolecules. 2012 Sep 10;13(9):2645-54. doi: 10.1021/bm300472y. Epub 2012 Aug 21.

Abstract

Peptide amphiphiles (PAs) self-assemble nanostructures with potential applications in drug delivery and tissue engineering. Some PAs share environmentally responsive behavior with their peptide components. Here we report a new type of PAs biologically inspired from human tropoelastin. Above a lower critical solution temperature (LCST), elastin-like polypeptides (ELPs) undergo a reversible inverse phase transition. Similar to other PAs, elastin-like PAs (ELPAs) assemble micelles with fiber-like nanostructures. Similar to ELPs, ELPAs have inverse phase transition behavior. Here we demonstrate control over the ELPAs fiber length and cellular uptake. In addition, we observed that both peptide assembly and nanofiber phase separation are accompanied by a distinctive secondary structure attributed primarily to a type-1 β turn. We also demonstrate increased solubility of hydrophobic paclitaxel (PAX) in the presence of ELPAs. Due to their biodegradability, biocompatibility, and environmental responsiveness, elastin-inspired biopolymers are an emerging platform for drug and cell delivery; furthermore, the discovery of ELPAs may provide a new and useful approach to engineer these materials into stimuli-responsive gels and drug carriers.

Publication types

  • Research Support, N.I.H., Extramural
  • Research Support, Non-U.S. Gov't

MeSH terms

  • Biocompatible Materials / chemical synthesis*
  • Biocompatible Materials / pharmacology
  • Biomimetic Materials / chemistry
  • Cell Survival / drug effects
  • Drug Carriers / chemical synthesis*
  • Drug Carriers / pharmacology
  • HEK293 Cells
  • HeLa Cells
  • Humans
  • Hydrophobic and Hydrophilic Interactions
  • Micelles
  • Microscopy, Atomic Force
  • Nanofibers / chemistry*
  • Nanofibers / ultrastructure
  • Paclitaxel / chemistry
  • Paclitaxel / pharmacology
  • Peptides / chemical synthesis*
  • Peptides / pharmacology
  • Phase Transition
  • Phosphatidylethanolamines / chemistry
  • Protein Structure, Secondary
  • Solubility
  • Surface-Active Agents / chemical synthesis*
  • Surface-Active Agents / pharmacology
  • Temperature
  • Tropoelastin / chemistry
  • Tubulin Modulators / chemistry
  • Tubulin Modulators / pharmacology

Substances

  • 1,2-dioleoyl-glycero-3-phosphatidyl ethanolamine
  • Biocompatible Materials
  • Drug Carriers
  • Micelles
  • Peptides
  • Phosphatidylethanolamines
  • Surface-Active Agents
  • Tropoelastin
  • Tubulin Modulators
  • Paclitaxel