Oppositely Charged Synthetic Peptides for Biomaterials with Immobilized Functional Proteins

Installs Folded Proteins into Supramolecular Assemblies that Demonstrate Properties Such As Molecular Recognition, Antigen Presentation, Tunable Drug Release, Catalysis or Fluorescence

This pair of synthetic peptides spontaneously self-assembles into a biomaterial with a precise supramolecular architecture with functional capabilities. The biomaterials market is expected to reach $150 billion by 2021. However, methods of producing advanced biomaterials with immobilized folded proteins remain a challenge, which limits opportunities to create biomaterials with advanced functional properties like catalysis, antigen conformation or molecular recognition.

Researchers at the University of Florida have developed a pair of oppositely charged synthetic peptides, called CATCH, or Co-Assembly Tags based on Charge-complementarity, to immobilize folded proteins into supramolecular biomaterials. Either of the CATCH peptides attaches to a protein of interest as a recombinant fusion tag. Proteins harboring a CATCH tag co-assemble with CATCH peptides into nanofibers, resulting in supramolecular biomaterials with a non-covalently immobilized protein displayed on their surface. The versatility of using a recombinant fusion tag for protein immobilization makes this platform potentially useful for various biomedical and biotechnological applications, including tissue engineering, regenerative medicine, drug delivery, immunotherapy, immunomodulation, and biosensing.

Application

A synthetic peptide pair that facilitates non-covalent protein immobilization into biomaterials for applications ranging from drug delivery to tissue engineering

Advantages

• Self-assembles into nanoscale architectures, creating functional supramolecular biomaterials with precise and reproducible composition
• Forms specific non-covalent bonds between proteins and biomaterials, leading to functional capabilities of biomaterials related to the protein
• Attaches to any desired folded protein, expanding its use to a broad number of biomedical and biotechnological applications

Technology

The CATCH peptides that form the basis for the supramolecular hydrogel can be synthesized and purified in high yield using both conventional solid-phase and recombinant expression methods. The latter provides a notable advantage over synthetic biomolecules capable of self-assembly. Because CATCH peptides co-assemble into ß-sheet nanofibers only when combined, due to electrostatic interactions, CATCH fusion proteins can be expressed and recovered from the soluble phase in exceptionally high yield and purity when compared to other platforms. CATCH peptides and fusion proteins can also be used to fabricate micron-sized particles or macroscopic hydrated gels by simply varying the composition of peptides and fusion proteins present during assembly.