Structural studies of collagen-like sequential polypeptides

Sequential polyhexapeptides, synthesised by combination of sequences from collagen type Gly-X-Y (X = Ala, Pro, Ser; Y = Ala, Gly, Lys, Pro), were characterized by the temperature dependence of circular dichroism spectra. Under comparable conditions these studies revealed that alternating triplets of Gly-Pro-Pro or Gly-Pro-Ala combined with Gly-Pro-Lys or Gly-Pro-Glu exhibit collagen-like structures in aqueous solutions. In case of unstructured chains of (Gly-Pro-Ala) ≈ 12 it can be shown that N-terminal crosslinking of three chains produces a similar ordered structure.