Design of synthetic collagens that assemble into supramolecular banded fibers as a functional biomaterial testbed
Jinyuan Hu,
Junhui Li,
Jennifer Jiang,
Lingling Wang,
Jonathan Roth,
Kenneth N. McGuinness,
Jean Baum,
Wei Dai,
Yao Sun (),
Vikas Nanda () and
Fei Xu ()
Additional contact information
Jinyuan Hu: Jiangnan University
Junhui Li: Shanghai Engineering Research Center of Tooth Restoration and Regeneration
Jennifer Jiang: The State University of New Jersey
Lingling Wang: Jiangnan University
Jonathan Roth: The State University of New Jersey
Kenneth N. McGuinness: The State University of New Jersey
Jean Baum: The State University of New Jersey
Wei Dai: The State University of New Jersey
Yao Sun: Shanghai Engineering Research Center of Tooth Restoration and Regeneration
Vikas Nanda: The State University of New Jersey
Fei Xu: Jiangnan University
Nature Communications, 2022, vol. 13, issue 1, 1-13
Abstract:
Abstract Collagens are the most abundant proteins of the extracellular matrix, and the hierarchical folding and supramolecular assembly of collagens into banded fibers is essential for mediating cell-matrix interactions and tissue mechanics. Collagen extracted from animal tissues is a valuable commodity, but suffers from safety and purity issues, limiting its biomaterials applications. Synthetic collagen biomaterials could address these issues, but their construction requires molecular-level control of folding and supramolecular assembly into ordered banded fibers, comparable to those of natural collagens. Here, we show an innovative class of banded fiber-forming synthetic collagens that recapitulate the morphology and some biological properties of natural collagens. The synthetic collagens comprise a functional-driver module that is flanked by adhesive modules that effectively promote their supramolecular assembly. Multiscale simulations support a plausible molecular-level mechanism of supramolecular assembly, allowing precise design of banded fiber morphology. We also experimentally demonstrate that synthetic fibers stimulate osteoblast differentiation at levels comparable to natural collagen. This work thus deepens understanding of collagen biology and disease by providing a ready source of safe, functional biomaterials that bridge the current gap between the simplicity of peptide biophysical models and the complexity of in vivo animal systems.
Date: 2022
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Persistent link: https://EconPapers.repec.org/RePEc:nat:natcom:v:13:y:2022:i:1:d:10.1038_s41467-022-34127-6
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DOI: 10.1038/s41467-022-34127-6
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