Prediction of Thermal Stability of Collagen Triple Helix

Invention Summary:

Collagens are the major structural proteins in the extracellular matrix of animals, including all vertebrates and invertebrates, and are defined by a characteristic triple-helix structure that requires a (Gly-Xaa-Yaa)n repeating sequence . Collagen is the most widely used biomaterial in a wide variety of biomedical applications including cosmetic surgery, tissue engineering, and drug delivery. For these applications, collagen is usually extracted from animal sources, especially bovines, but there has been a growing concern of transmissible diseases from these sources. Other concerns include the lack of standardization for extracted bovine collagen preparations and an inability to make any modifications to the sequence to improve biological properties. Therefore, synthetic triple-helical peptides that mimic the structure of collagens can be very important.  Crystal structures of collagen peptides show that variation in amino acid content along the (Gly-X-Y)n sequence leads to small but significant variations in the superhelix twist resulting in thermally liable and stable regions. Therefore amino acid sequence of the triple helical construct is critical in defining the thermal stability of the designed triple helix, which can be useful for a clinical or related applications.

Rutgers Researchers have developed a method to determine the prediction of thermal stability of designed triple helical sequences.  This method comprisesan algorithm that allows the prediction of thermal stability for designed triple helical sequences, so that the thermal stability of novel constructs or variations on natural sequences can be optimized for the desired performance characteristics of the product(s). This calculation is based on the triple-helical stabilization propensities of individual residues and their intermolecular and intramolecular interactions, as quantitated by melting temperature values of host-guest peptides. Application of the algorithm to collagen sequences highlights regions of unusually high or low stability, and these regions often correlate with biologically significant features.

Market Applications:

Prediction of thermal stability of designed collagen like triple helical peptides to determine whether they can be used for Biomedical applications.

Intellectual Property & Development Status:

United States patent number 8,280,710 granted on October 2, 2012

Rutgers ID: S05-04
Life Sciences
Lisa Lyu
Licensing Manager
Barbara Brodsky
Anton Persikov
John Ramshaw