A flexible membrane templating technique (a) is developed for the fabrication of microcrimped collagen microfibers (b) that are embedded in an elastin‐like protein matrix to generate hierarchical, biologically inspired fiber‐reinforced composites (c). The microcrimped structure is stable under cyclic loading and the mechanical response of the engineered collagen‐elastin composite mimics that of native tissue.

The unique biomechanical properties of native tissue are governed by the organization and composition of integrated collagen and elastin networks. We report an approach for fabricating spatially aligned, fiber-reinforced composites (FRC) with adjustable collagen fiber dimensions, layouts, and distribution within an elastin-like protein matrix yielding a biocomposite with controllable mechanical responses. Microtransfer molding is employed for the fabrication of hollow and solid collagen fibers with straight or crimped fiber geometries. Collagen fibers (width: 2 – 50 μm, thickness: 300 nm – 3 μm) exhibit a Young’s modulus of 126 ± 61 MPa and an ultimate tensile strength (UTS) of 7 ± 3.2 MPa. As fiber networks within composite structures, straight fiber layouts display orthotropic responses with Young’s modulus ranging from 0.95 ± 0.35 to 10.4 ± 0.5 MPa and tensile strength from 0.22 ± 0.08 to 0.87 ± 0.5 MPa with increasing fraction of collagen fibers (1–10% v/v). In contrast, composites based on crimped fiber layouts exhibit strain-dependent stiffness with an increase in Young’s modulus from 0.7 ± 0.14 MPa to 3.15 ± 0.49 MPa, at a specific transition strain. Through controlling the microstructure of engineered collagen fiber networks, a facile means has been established to control macroscale mechanical responses of composite protein-based materials.

Noting the abundance and importance of collagen as a biomaterial, we have developed a facile method for the production of dense fibrillar extracellular matrix mimicking collagen-elastin hybrids with tunable mechanical properties. Through the use of excimer laser technology, we have optimized conditions for the ablation of collagen lamellae without denaturation of protein, maintenance of fibrillar ultrastructure and preservation of native D-periodicity. Strengths of collagen-elastin hybrids ranged from 0.6 - 13 MPa, elongation at break from 9 - 70 %, and stiffness from 2.9 - 94 MPa, allowing for the design of a wide variety of tissue specific scaffolds. Further, large (centimeter scale) lamellae can be fabricated and embedded with recombinant elastin to generate collagen-elastin hybrids. Exposed collagen in hybrids act as cell adhesive sites for rat mesenchymal stem cells that conform to ablate waveforms. The ability to modulate these features allows for the generation of a class of biopolymers that can architecturally and physiologically replicate native tissue.