Divalent metal ion modulation of a simple peptide-based hydrogel: self-assembly and viscoelastic properties.

Peptide self-assembly has been highly studied to understand the pathways in forming higher order structures along with the development and application of resulting hydrogel materials. Driven by noncovalent interactions, peptide hydrogels are stimuli-responsive to any addition to its gelling conditions. Here, a Phe-His based peptide, C14-FH(Trt)-OH, was synthesized and characterized with 1H NMR, FT-IR, MS, UV-vis spectroscopies and elemental analysis. Based on SEM imaging, the dipeptide conjugate was capable of forming a nanofibrous, interconnected network encapsulating buffer to produce a supramolecular hydrogel. Through the addition of Zn2+ and Cu2+, there is a clear change in the self-assembled nanostructures characterized through SEM. With this effect on self-assembly follows a change in the viscoelastic properties of the material, as determined through rheological frequency sweeps, with 2 and 3 orders of magnitude decreases in the elastic modulus G' in the presence of Zn2+ and Cu2+ respectively. This highlights the tunability of soft material properties with peptide design and self-assembly, through metal ions and Nδ-directed coordination.

Multi-component peptide hydrogels - a systematic study incorporating biomolecules for the exploration of diverse, tuneable biomaterials.

Peptide-based supramolecular gels can be designed to be functional "smart" materials that have applications in drug delivery, tissue engineering, and supramolecular chemistry. Although many multi-component gel systems have been designed and reported, many of these applications still rely solely on single-component gel systems which limits the functionalities of the materials. Multi-component self-assembly leads to the formation of highly ordered and complex architectures while offering the possibility to generate hydrogels with interesting properties including functional complexity and diverse morphologies. Being able to incorporate various classes of biomolecules can allow for tailoring the materials' functionalities to specific application needs. Here, a novel peptide amphiphile, myristyl-Phe-Phe (C14-FF), was synthesized and explored for hydrogel formation. The hydrogel possesses a nanofiber matrix morphology, composed of ß-sheet aggregates, a record-low gelation concentration for this class of compounds, and a unique solvent-dependent helical switch. The C14-FF hydrogel was then explored with various classes of biomolecules (carbohydrates, vitamins, proteins, building blocks of HA) to generate a multi-component library of gels that have potential to represent the complex natural extracellular matrix. Selected multi-component gels exhibit an excellent compatibility with mesenchymal stem cells showing high cell viability percentages, which holds great promise for applications in regenerative therapy.

Supramolecular Peptide Gels: Influencing Properties by Metal Ion Coordination and Their Wide-Ranging Applications.

Supramolecular gels have been an area of interest in many research fields. They provide a means to understand assembly of nanostructures, and through the use of amino acid- and peptide-based gelators they can give insights into the similar assembly pathways of their more complex structural counterparts. Bio-inspired metal coordination, such as histidine-copper coordination, in the supramolecular assembly of these gelators is one method for furthering our understanding and development of these materials. Metal-gelator coordination mimics biologically relevant metal-peptide coordination, thus influencing hydrogel self-assembly and mechanical properties, including biodegradability, biocompatibility, tunability, and recyclablity, while the metal coordination can functionalize the gels to allow for widespread applications in biomedical industries (e.g., drug delivery), waste management, and catalysis. This review aims to discuss recent insights into the supramolecular assembly of gels involving metal ions, as well as a few key areas of application using metal interactions and incorporation.

Enzyme Entrapment in Amphiphilic Myristyl-Phenylalanine Hydrogels.

Supramolecular amino acid and peptide hydrogels are functional materials with a wide range of applications, however, their ability to serve as matrices for enzyme entrapment have been rarely explored. Two amino acid conjugates were synthesized and explored for hydrogel formation. These hydrogels were characterized in terms of strength and morphology, and their ability to entrap enzymes while keeping them active and reusable was explored. It was found that the hydrogels were able to successfully entrap two common and significant enzymes-horseradish peroxidase and -amylase-thus keeping them active and stable, along with inducing recycling capabilities, which has potential to further advance the industrial biotransformation field.