title: Tuning of collagen triple-helix stability in recombinant telechelic polymers.
abstract: The melting properties of various triblock copolymers with random coil middle blocks (100-800 amino acids) and triple helix-forming (Pro-Gly-Pro)(n) end blocks (n = 6-16) were compared. These gelatin-like molecules were produced as secreted proteins by recombinant yeast. The investigated series shows that the melting temperature (T(m)) can be genetically engineered to specific values within a very wide range by varying the length of the end block. Elongation of the end blocks also increased the stability of the helices under mechanical stress. The length-dependent melting free energy and T(m) of the (Pro-Gly-Pro)(n) helix appear to be comparable for these telechelic polymers and for free (Pro-Gly-Pro)(n) peptides. Accordingly, the T(m) of the polymers appeared to be tunable independently of the nature of the investigated non-cross-linking middle blocks. The flexibility of design and the amounts in which these nonanimal biopolymers can be produced (g/L range) create many possibilities for eventual medical application.
authors.affiliation: Wageningen UR Food & Biobased Research , Bornse Weilanden 9, NL-6708 WG Wageningen, The Netherlands. catarinaifsilva@gmail.com
authors.forename: Catarina I F
authors.initials: CI
authors.lastname: Silva
authors.forename: Paulina J
authors.initials: PJ
authors.lastname: Skrzeszewska
authors.forename: Monika D
authors.initials: MD
authors.lastname: Golinska
authors.forename: Marc W T
authors.initials: MW
authors.lastname: Werten
authors.forename: Gerrit
authors.initials: G
authors.lastname: Eggink
authors.forename: Frits A
authors.initials: FA
authors.lastname: de Wolf
mesh_terms: D001704:Biopolymers / Q000737:chemistry* / Q000235:genetics; D003094:Collagen / Q000737:chemistry*; D005818:Genetic Engineering; D008958:Models, Molecular; D055550:Protein Stability; D017433:Protein Structure, Secondary; D011994:Recombinant Proteins / Q000737:chemistry / Q000235:genetics
chemical_list: D001704:Biopolymers; D011994:Recombinant Proteins; D003094:Collagen