Abstract: Novel peptidomimetics are provided, which mimic collagen. Molecular structures of interest include for imparting the collagen-mimicking property are each of: Gly-?[(E)CH?C]-Xaa-?[(E)CH?C]-Yaa; Gly-Xaa-?[(E)CH?C]-Yaa; Gly-Xaa-Yaa-?[(E)CH?CH]; Gly-?[(E)CH?C]-Xaa-?[(E)CH?C]-Yaa; Gly-Xaa-?(E)CH?C]-Yaa-?[(E)CH?CH]; Gly-?[(E)CH?C]-Xaa-Yaa-?[(E)CH?CH] and Gly-?[(E)CH?C]-Xaa-?[(E)CH?C]-Yaa-?[(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.

Abstract: Novel collagen mimics are disclosed with a tripeptide unit having the formula (Xaa-Yaa-Gly)n, where one of the positions Xaa or Yaa is a bulky, non-electron withdrawing proline derivative. By substituting a proline derivative at either the Xaa or Yaa position in the native collagen helix, the stability of the helix is increased due solely to steric effects relative to prior known collagen-related triple helices. Methods are also disclosed for making the novel collagen mimics.