4 research outputs found
Tuning of Collagen Triple-Helix Stability in Recombinant Telechelic Polymers
The melting properties of various triblock copolymers
with random coil middle blocks (100–800
amino acids) and triple helix-forming (Pro-Gly-Pro)<sub><i>n</i></sub> end blocks (<i>n</i> = 6–16) were compared.
These gelatin-like molecules were produced as secreted proteins by
recombinant yeast. The investigated series shows that the melting
temperature (<i>T</i><sub>m</sub>) 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 <i>T</i><sub>m</sub> of the (Pro-Gly-Pro)<sub><i>n</i></sub> helix appear to be comparable for these
telechelic polymers and for free (Pro-Gly-Pro)<sub><i>n</i></sub> peptides. Accordingly, the <i>T</i><sub>m</sub> 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