Poly(l-proline)-Stabilized Polypeptide Nanostructures via Ring-Opening Polymerization-Induced Self-Assembly (ROPISA).
Ernesto Tinajero-DíazNicola JudgeBo LiThomas LeighRobert D MurphyPaul D TophamMatthew J DerryAndreas HeisePublished in: ACS macro letters (2024)
Poly(proline) II helical motifs located at the protein-water interface stabilize the three-dimensional structures of natural proteins. Reported here is the first example of synthetic biomimetic poly(proline)-stabilized polypeptide nanostructures obtained by a straightforward ring-opening polymerization-induced self-assembly (ROPISA) process through consecutive N -carboxyanhydride (NCA) polymerization. It was found that the use of multifunctional 8-arm initiators is critical for the formation of nanoparticles. Worm-like micelles as well as spherical morphologies were obtained as confirmed by dynamic light scattering (DLS), transmission electron microscopy (TEM), and small angle X-ray scattering (SAXS). The loading of the nanostructures with dyes is demonstrated. This fast and open-vessel procedure gives access to amino acids-based nanomaterials with potential for applications in nanomedicine.
Keyphrases
- electron microscopy
- high resolution
- high glucose
- amino acid
- drug delivery
- cancer therapy
- diabetic rats
- minimally invasive
- drug induced
- risk assessment
- magnetic resonance imaging
- endothelial cells
- oxidative stress
- mass spectrometry
- climate change
- small molecule
- drug release
- hyaluronic acid
- binding protein
- human health
- stress induced
- bone regeneration