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Tuning of Collagen Triple-Helix Stability in Recombinant Telechelic Polymers

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journal contribution
posted on 14.05.2012, 00:00 by Catarina I. F. Silva, Paulina J. Skrzeszewska, Monika D. Golinska, Marc W. T. Werten, Gerrit Eggink, Frits A. de Wolf
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 (Tm) 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 Tm 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 Tm 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.