Higher-order assembly of collagen peptides into nano- and microscale materials.
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.
Przybyla
David E
DE
Department of Chemistry, Purdue University, 560 Oval Drive, West Lafayette, Indiana 47907, USA.
Chmielewski
Jean
J
D001672:Biocompatible Materials / Q000032:analysis / Q000737:chemistry* / Q000378:metabolism; D003094:Collagen / Q000032:analysis / Q000737:chemistry*; D016503:Drug Delivery Systems / Q000009:adverse effects; D005109:Extracellular Matrix / Q000737:chemistry* / Q000378:metabolism; D008420:Manufactured Materials / Q000032:analysis; D010455:Peptides / Q000032:analysis / Q000737:chemistry* / Q000378:metabolism*; D023822:Tissue Engineering / Q000379:methods
D001672:Biocompatible Materials; D010455:Peptides; D003094:Collagen