Biomimetic Self-Templated Hierarchical Structures of Collagen-Like Peptide Amphiphiles.
basic_science · Level V
Where this comes from
- Record sourced from PubMed, PMID 26392232.
- Also identified by DOI 10.1021/acs.nanolett.5b03313.
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Abstract
Developing hierarchically structured biomaterials with tunable chemical and physical properties like those found in nature is critically important to regenerative medicine and studies on tissue morphogenesis. Despite advances in materials synthesis and assembly processes, our ability to control hierarchical assembly using fibrillar biomolecules remains limited. Here, we developed a bioinspired approach to create collagen-like materials through directed evolutionary screening and directed self-assembly. We first synthesized peptide amphiphiles by coupling phage display-identified collagen-like peptides to long-chain fatty acids. We then assembled the amphiphiles into diverse, hierarchically organized, nanofibrous structures using directed self-assembly based on liquid crystal flow and its controlled deposition. The resulting structures sustained and directed the growth of bone cells and hydroxyapatite biominerals. We believe these self-assembling collagen-like amphiphiles could prove useful in the structural design of tissue regenerating materials.
Medical subject headings
- Biomimetics
- Collagen
- Peptides