Multiscale characterization of a chimeric biomimetic polypeptide for stem cell culture

Abstract

Mesenchymal stem cells have attracted great interest in the field of tissue engineering and regenerative medicine because of their multipotentiality and relative ease of isolation from adult tissues. The medical application of this cellular system requires the inclusion in a growth and delivery scaffold that is crucial for the clinical effectiveness of the therapy. In particular, the ideal scaffolding material should have the needed porosity and mechanical strength to allow a good integration with the surrounding tissues, but it should also assure high biocompatibility and full resorbability. For such a purpose, protein-inspired biomaterials and, in particular, elastomeric-derived polypeptides are playing a major role, in which they are expected to fulfil many of the biological and mechanical requirements. A specific chimeric protein, designed starting from elastin, resilin and collagen sequences, was characterized over different length scales. Single-molecule mechanics, aggregation properties and compatibility with human mesenchymal stem cells were tested, showing that the engineered compound is a good candidate as a stem cell scaffold to be used in tissue engineering applications.

Protein‐based functional nanomaterial design for bioengineering applications

“…As expected, the individual REC chains have shown exceptional extensibility along with the self‐assembling properties resulting from collagen‐like domains . RECs self‐assemble into fibrous aggregates that support cell proliferation as shown with primary human MSCs . The cell alignment is also shown to be affected by the orientation of the underlying fibers giving the materials a potential to physically influence cell behavior and increases their value as tissue engineering scaffolds.…”

“…Unlike the silk–collagen‐like chimeric polypeptides with rigid, self‐assembling silk and bioactive or random coil collagen‐like domains, the more recently established resilin–elastin–collagen‐like polypeptides (RECs) are composed of flexible resilin and elastin domains along with rigid, self‐assembling collagen‐like domains . As expected, the individual REC chains have shown exceptional extensibility along with the self‐assembling properties resulting from collagen‐like domains . RECs self‐assemble into fibrous aggregates that support cell proliferation as shown with primary human MSCs .…”

Recombinant Technology in the Development of Materials and Systems for Soft‐Tissue Repair

“…One example of the improvement obtained by way of such rational design is the synthesis of amphiphilic block co‐polymers that spontaneously self‐assemble to form continuous hydrogels for use as tissue‐engineering scaffolds that have been cast with a defined and controlled topography . In this way, the physical properties, stimuli‐responsiveness and mechanical behavior are tuned and additional biofunctionalities included, thereby resulting in customized materials to control specific functions or to elicit tissue regeneration . This tissue regeneration is guided by the association between cells and their ECM, a bi‐directional and dynamic interaction that activates intracellular signaling pathways .…”

Recent Contributions of Elastin-Like Recombinamers to Biomedicine and Nanotechnology

“…Moreover, their characteristics make them biomimetic and re-absorbable materials with a defined mechanical behavior [25,26] that allows them to be cast with a specific topography [27,28] whilst retaining their tunable temperature responsiveness [29] and controlled structural features. ELR sequences based on the repetition of certain modular ECM structural protein motifs allow the physicochemical [10], mechanical [30], and biological [31] properties of the natural proteins from which they are derived to be reproduced [32]. These properties have made ELRs one of the materials of choice when investigating new biomaterials for biomedical applications.…”