Chemical modifications to strengthen and stabilize collagen for biomaterials and biomedicine
Unnatural amino acid substitution for hyperstable collagen-based materials
The Chenoweth Lab has discovered an unnatural amino acid substitution in collagen to dramatically improve the strength and stability of collagen for a wide range of biomaterial and biomedical applications. More specifically, the researchers have created a new class of collagen mimetic peptides with an unnatural amino acid substitution of aza-glycine that stabilizes the triple helical structure of collagen via increasing the number of interfacial hydrogen bonds, improving the material’s strength.
Collagen is the most abundant protein in mammals, present in tendons, ligaments, cartilage, bones, blood vessels, skin, and tissue. Hydrogen bonding is critical in maintaining structural integrity in natural biopolymer systems, so it is advantageous to maximize the number of hydrogen bonds with minimal perturbation to the structure and function of the biomolecule.
This report is the first atomic modification to the main chain backbone of collagen to affect glycine, the result of which yields triple helix hyperstability and significantly faster folding kinetics.
- Improved strength and stability of collagen
- Faster folding kinetics
- Maximize number of hydrogen bonds within collagen
- Self-assembling biomimetic materials
- Cosmetics and cosmeceuticals
- Skin grafts, wound healing
- Cosmetic/plastic surgery
- Joint repair
- Tissue engineering and regenerative medicine
- Drug delivery
Stage of Development:
Reduction to Practice
US Utility Pending
- Kasznel et al. JACS, 2017, 139, pgs. 9427-9430.
- Zhang et al. JACS, 2016, 138, pgs. 9751-9754.
- Zhang et al. JACS, 2015, 137(39) pgs 12422-12425.
- Highlight in News of the Week, Chemical and Engineering News, 2015, 93(38), pg. 7.
- Highlight in Penn Current, 2015