| abstract |
Novel peptidomimetics are provided, which mimic collagen. Molecular structures of interest include for imparting the collagen-mimicking property are each of: Gly- Ψ[(E)CH=C]-Xaa-Yaa; Gly-Xaa-Ψ[(E)CH=C]-Yaa; Gly-Xaa-Yaa-Ψ[(E)CH=CH]; Gly- Ψ[(E)CH=C]-Xaa-Ψ[(E)CH=C]-Yaa; Gly-Xaa-Ψ(E)CH=C]-Yaa-Ψ[(E)CH=CH]; Gly-Ψ[(E)CH=C]-Xaa-Yaa-Ψ[(E)CH=CH] and Gly-Ψ[(E)CH=C]-Xaa-Ψ[(E)CH=C]-Yaa-Ψ[(E)CH=CH]. Xaa and Yaa each means a natural amino acid, Hyp or Flp. Amide bonds may be altered to create collagen mimics. Preferably a tripeptide polymer comprising at least about 60 (Gly-Pro-Hyp) repeating units and having molecular weight of at least about 40,000 is synthesized as a long, collagen-like material. The new synthetic collagen-like materials may have better resistance to degradation, better mechanical strength and/or better ability to fold than natural collagen. |