Chemical Engineering Seminar

We discovered that rationally designed ultrashort aliphatic peptides consisting of just 3-6 aliphatic amino acids with an innate tendency to easily self-assemble in water into helical fibers give rise to fibrous scaffolds and vesicle-like nanoparticles with unique physico-chemical properties. The resulting fiber nanotopography and the entangled fibrous supramolecular networks forming hydrogels show properties comparable to that of collagen and ECM-like material. Peptide hydrogels are ideal candidates for biomedical applications, since they resemble natural proteins, show chemical versatility, functionalization potential, intrinsic biocompatibility and biodegradability.  We have explored these hydrogels as smart biomaterials for a range of biomedical applications, in particular for regenerative medicine and tissue engineering, but also for drug delivery, bioimaging and topical applications. Functionalization and cross-linking further support cell viability and spreading in a true 3D distribution. Interestingly, a subclass of lysine-containing peptides exhibit instantaneous gelation in the presence of salts. Combined with excellent tunable mechanical properties, it supports their use for injectable therapies, three-dimensional bio-printing and molding. Exploiting this property, we developed an alternative, minimally invasive treatment for degenerative disc disease. This injectable therapy is considerably less invasive compared to the surgical alternatives available in the clinic today. We also investigated the peptide hydrogels as wound dressings for burn wound in a rat model. Furthermore, the mechanical properties can be modulated to match that of native tissue, which is suitable for bioprinting of organotypic tissue. The in vivo stability, amenability to standard sterilization procedures and incorporation of contrast agents, cells and other biochemical cues enable these self-assembled peptide hydrogels as an excellent biomaterial for clinical use.