Abstract
Synthetically derived peptide-based biomaterials are in many instances capable of mimicking the structure and function of their full-length endogenous counterparts. Combine this with the fact that short mimetic peptides are easier to produce when compared to full length proteins, show enhanced processability and ease of modification, and have the ability to be prepared under well-defined and controlled conditions; it becomes obvious why there has been a recent push to develop regenerative biomaterials from these molecules. There is increasing evidence that the incorporation of peptides within regenerative scaffolds can result in the generation of structural recognition motifs that can enhance cell attachment or induce cell signaling pathways, improving cell infiltration or promote a variety of other modulatory biochemical responses. By highlighting the current approaches in the design and application of short mimetic peptides, we hope to demonstrate their potential in soft-tissue healing while at the same time drawing attention to the advances made to date and the problems which need to be overcome to advance these materials to the clinic for applications in heart, skin, and cornea repair.
Highlights
Bioinspired materials for tissue repair have been amongst the most exhaustively explored fields in biomaterials research, yet mimicry of native extra cellular matrix (ECM), remains one of the most challenging tasks in tissue engineering
While remarkable progress in recombinant protein expression has been made, there remains a gap as these processes are still relatively expensive for heteromeric proteins; limiting scientists to the use animal origin proteins including collagen and elastin for engineering translatable biomaterials
Difficult peptide sequences refer to peptide sequences that agglomerate forming insoluble products during synthesis or after removal of the protective groups, a process that results in reduced yields or deactivation of the peptide preventing further modifications (Tickler and Wade, 2007)
Summary
Bioinspired materials for tissue repair have been amongst the most exhaustively explored fields in biomaterials research, yet mimicry of native extra cellular matrix (ECM), remains one of the most challenging tasks in tissue engineering. Peptide-Based Biomaterials synthesis and the recombinant production of full length proteins and peptides, generating and studying the interactions of mimetic molecules has been greatly simplified Whether it is the production of exact copies of full-length or fragments of proteins, the incorporation of non-coded amino acids, or modification of the peptide backbone to enhance its proteolytic stability or the inclusion of tethers for further functionalization; one can generally find a suitable method to produce the desired molecule. Difficult peptide sequences refer to peptide sequences that agglomerate forming insoluble products during synthesis or after removal of the protective groups, a process that results in reduced yields or deactivation of the peptide preventing further modifications (Tickler and Wade, 2007) In most instance these problems arise due to introduction of functionalities capable a participating in non-covalent interactions, such as hydrogen bonds and dipole-dipole interactions (Paradis-Bas et al, 2016). The angiogenic properties of peptide QK have been demonstrated both in vitro and in vivo, with evident endothelial cell activation and increases in VEGF related cellular functions such as chemotaxis, invasion, sprouting of new capillaries, and enhanced organization (Andrea et al, 2005; Finetti et al, 2012)
Sign-in/Register to view highlights & summary Talk to us
Join us for a 30 min session where you can share your feedback and ask us any queries you have
Schedule a callDisclaimer: All third-party content on this website/platform is and will remain the property of their respective owners and is provided on "as is" basis without any warranties, express or implied. Use of third-party content does not indicate any affiliation, sponsorship with or endorsement by them. Any references to third-party content is to identify the corresponding services and shall be considered fair use under The CopyrightLaw.
