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, t...

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Bibliographic Details
Published inBiochemistry (Easton) Vol. 49; no. 21; pp. 4411 - 4419
Main Authors Przybyla, David E, Chmielewski, Jean
Format Journal Article
LanguageEnglish
Published United States American Chemical Society 01.06.2010
Subjects
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
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Summary: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.
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ISSN:0006-2960
1520-4995
DOI:10.1021/bi902129p