| Name: | Description: | Size: | Format: | |
|---|---|---|---|---|
| 1.92 MB | Adobe PDF |
Advisor(s)
Abstract(s)
Peptides can be designed to recreate the higher-order assembly (triple helix) and biological function of natural collagens. Collagen triple-helical domain contains Gly-Xaa-Yaa triplets where Xaa and Yaa are frequently proline and hydroxyproline, respectively. Glycine must be in every third position forming a hydrogen bond to an adjacent proline to stabilize collagen structure. Hydroxyproline residues are important in the thermal stability of the collagen triple-helix conformation. Although it is difficult to produce a stable triple helix, collagen-like peptides can be used to produce scaffolds that mimic natural tissue networks for biomedical engineering, without the liabilities of nonhuman natural collagens such us immunogenicity and pathogen transmission. This chapter describes the major approaches towards synthesis of collagen-like peptides, essentially aimed at production of artificial biocompatible and biofunctional frameworks for regenerative medicine.
Description
Keywords
Collagen Chemical synthesis Extracellular matrix Fibril Hydroxyproline Peptide Protein Regenerative medicine Triple helix
Citation
Teixeira, C., Ferraz, R., Prudêncio, C., & Gomes, P. (2018). 11—Collagen-like materials for tissue regeneration and repair. Em M. A. Barbosa & M. C. L. Martins (Eds.), Peptides and Proteins as Biomaterials for Tissue Regeneration and Repair (pp. 283–307). Woodhead Publishing. https://doi.org/10.1016/B978-0-08-100803-4.00011-5
Publisher
Elsevier