Higher-order assembly of collagen peptides into nano- and microscale materials

Biochemistry. 2010 Jun 1;49(21):4411-9. doi: 10.1021/bi902129p.

Abstract

The triple-helical structure of collagen peptides has recently been harnessed as a subunit in the higher-order assembly of unique biomaterials. Specific assembly signals have been designed within collagen peptides, including hydrophobic groups, electrostatic interactions, and metal-ligand binding, to name a few. In this way, a range of novel assemblies have been obtained, including nano- to microscale fibers, gels, spheres, and meshes, each with the potential for novel biological applications in drug delivery, tissue engineering, and regenerative medicine.

Publication types

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

MeSH terms

  • Biocompatible Materials / analysis
  • Biocompatible Materials / chemistry*
  • Biocompatible Materials / metabolism
  • Collagen / analysis
  • Collagen / chemistry*
  • Drug Delivery Systems / adverse effects
  • Extracellular Matrix / chemistry*
  • Extracellular Matrix / metabolism
  • Manufactured Materials / analysis
  • Peptides / analysis
  • Peptides / chemistry*
  • Peptides / metabolism*
  • Tissue Engineering / methods

Substances

  • Biocompatible Materials
  • Peptides
  • Collagen