A Comparison of the Mechanical Properties of ECM Components and Synthetic Self-Assembling Peptides.
review · Level V
Where this comes from
- Record sourced from PubMed, PMID 39972630.
- Also identified by DOI 10.1002/adhm.202402385 and PMC identifier 12023840.
- Licence recorded as CC BY.
- The licence permits redistribution, so the abstract is shown in full and the full text is available from the publisher.
Abstract
The field of tissue engineering is increasingly moving away from a one-size-fits-all approach of simple synthetic homogeneous gels, and embracing more tailored designs to optimize cell function and differentiation for the organ of interest. Extracellular matrix (ECM) proteins are still the optimal route for controlling cell function, while a field of great promise is that of synthetic self-assembling peptides (SSAPs), which are fully biocompatible, biodegradable, and offer both the hierarchical structure and dynamic properties displayed by protein networks found in natural tissue. However, the mechanical properties of neither group have been comprehensively reviewed. In this review, rheological data and the Young's modulus of the most prevalent proteins involved in the ECM (collagen I, elastin, and fibronectin) are collated for the first time, and compared against the most widely researched SSAPs: peptide amphiphiles (PAs), β-sheets, β-hairpin peptides, and Fmoc-based gels (with a focus on PA-E3, RADA16, MAX1, and FmocFF, respectively).
Medical subject headings
- Peptides
- Extracellular Matrix
- Extracellular Matrix Proteins