title: Collagen mimetic dendrimers.
abstract: The synthesis of single-chain, scaffold (TRIS)- and dendrimer-assembled collagen mimetics (both Gly-Pro-Nleu and Gly-Nleu-Pro sequences) is reported. From the CD spectra and the thermal denaturation studies it can be readily seen that mimetics prepared from the Gly-Nleu-Pro sequence form more thermally stable triple helices than the Gly-Pro-Nleu sequence. Furthermore, the 162-residue collagen mimetic dendrimers exhibit enhanced triple helical stability compared to equivalent scaffold-terminated structures by a substantial increase in the melting temperature in H2O and 2:1 EG/H2O. The concentration dependence for the melting transition was measured which determined that the stabilization effect arises from the intramolecular clustering of the triple helical arrays about the core structure. This ensemble excludes solvent from the interior portion of the array which stabilizes the triple helical bundle.
authors.affiliation: Department of Chemistry and Biochemistry, University of California - San Diego, La Jolla, California 92093, USA.
authors.forename: Garth A
authors.initials: GA
authors.lastname: Kinberger
authors.forename: Weibo
authors.initials: W
authors.lastname: Cai
authors.forename: Murray
authors.initials: M
authors.lastname: Goodman
mesh_terms: D040761:Biomimetic Materials / Q000138:chemical synthesis / Q000737:chemistry*; D002942:Circular Dichroism; D003094:Collagen / Q000737:chemistry*; D006358:Hot Temperature; D009842:Oligopeptides / Q000138:chemical synthesis / Q000737:chemistry*; D011487:Protein Conformation; D011489:Protein Denaturation
chemical_list: D009842:Oligopeptides; D003094:Collagen