Peptide-directed self-assembly of hydrogels

Acta Biomater. 2009 Mar;5(3):805-16. doi: 10.1016/j.actbio.2008.10.001. Epub 2008 Oct 14.

Abstract

This review focuses on the self-assembly of macromolecules mediated by the biorecognition of peptide/protein domains. Structures forming alpha-helices and beta-sheets have been used to mediate self-assembly into hydrogels of peptides, reactive copolymers and peptide motifs, block copolymers, and graft copolymers. Structural factors governing the self-assembly of these molecules into precisely defined three-dimensional structures (hydrogels) are reviewed. The incorporation of peptide motifs into hybrid systems, composed of synthetic and natural macromolecules, enhances design opportunities for new biomaterials when compared to individual components.

Publication types

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

MeSH terms

  • Biocompatible Materials / chemistry
  • Hydrogels / chemistry*
  • Models, Chemical
  • Molecular Conformation
  • Peptides / chemistry*
  • Polymers / chemistry
  • Protein Structure, Secondary
  • Protein Structure, Tertiary
  • Proteins / chemistry

Substances

  • Biocompatible Materials
  • Hydrogels
  • Peptides
  • Polymers
  • Proteins