Direct Synthesis of a Covalently Self-Assembled Peptide Nanogel from a Tyrosine-Rich Peptide Monomer and Its Biomineralized Hybrids

Angew Chem Int Ed Engl. 2018 May 14;57(20):5630-5634. doi: 10.1002/anie.201713261. Epub 2018 Apr 23.

Abstract

There has been significant progress in the self-assembly of biological materials, but the one-step covalent peptide self-assembly for well-defined nanostructures is still in its infancy. Inspired by the biological functions of tyrosine, a covalently assembled fluorescent peptide nanogel is developed by a ruthenium-mediated, one-step photo-crosslinking of tyrosine-rich short peptides under the visible light within 6 minutes. The covalently assembled peptide nanogel is stable in various organic solvents and different pH levels, unlike those made from vulnerable non-covalent assemblies. The semipermeable peptide nanogel with a high density of redox-active tyrosine acts as a novel nano-bioreactor, allowing the formation of uniform metal-peptide hybrids by selective biomineralization under UV irradiation. As such, this peptide nanogel could be useful in the design of novel nanohybrids and peptidosomes possessing functional nanomaterials.

Keywords: covalent self-assembly; metal-peptide hybrids; nanogels; peptides; tyrosine.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Biomineralization
  • Molecular Structure
  • Nanogels
  • Particle Size
  • Peptides / chemical synthesis*
  • Peptides / chemistry
  • Polyethylene Glycols / chemical synthesis*
  • Polyethylene Glycols / chemistry
  • Polyethyleneimine / chemical synthesis*
  • Polyethyleneimine / chemistry
  • Surface Properties
  • Tyrosine / chemistry*

Substances

  • Nanogels
  • Peptides
  • polyethylene glycol polyethyleneimine nanogel
  • Polyethylene Glycols
  • Tyrosine
  • Polyethyleneimine