Elastic protein-based polymers response

Only because the remarkable biocompatibility of chemically synthesized poly(GVGVP) was already known was there adequate impetus to purify microbially prepared (GVGVP)2si. Otherwise, it would have been presumed, as had been widely expected, that the toxicity of inadequately purified (GVGVP)25i was an inherent property of the protein-based polymer. To be left in such a state of misunderstanding would have meant that the dramatic potential of elastic protein-based polymers for use in medical applications would be neither appreciated nor realized. The inflammatory response elicited by an inadequately purifled biosynthetic elastic protein-based polymer would have overwhelmed most considered medical applications. 

S.3 Response of Human Monocytes to Elastic Protein-based Polymers... 

When seeking an optimal biomaterial, the preference is for complete absence of toxicity on placement in the host. With such a totally innocuous elastic protein-based biomaterial, biologically active sequences can be readily included within the polymer, and the host tissue can react to the biologically active sequence without being overwhelmed by unwanted reactions. Thus, because of the high level of biocompatibility, there exists the capacity to elicit diverse and desired tissue responses. 

Uny et also reported the chemical synthesis of protein polymers based on the (Val-Pro- Ala-Val-Gly) repeat sequence in which glycine is replaced by the D-alanine residue. The hetero-chiral Pro- Ala diad would be erqrected on the basis of stereochemical considerations to adopt a type-II p-tum conformation. Stmctural analyses of small-molecule "Pro- Ala turn models support the formation of the type-II p-mm conformation in solution and the solid state. Polymers based on the (Val-Pro- Ala-Val-Gly) repeat sequence display a thermo-reversible phase transition similar to the corresponding polypeptides derived from the parent (Val-Pro-Gly-Val-Gly) sequence, albeit with a shift of the Tt to approximately 5-10 ° G below the latter due to a slight inaease in hydrophobic character due to the presence of the alanine residue. NMR spectroscopic analyses of the (Val-Pro- Ala-Val-Gly) polymer suggest that the repeat unit retains the p-tum stmcture on the basis of comparison to the corresponding behavior of the (Val-Pro-Gly-Val-Gly) polymer. Stress-strain measurements on cross-linked matrices of the (Val-Pro- Ala-Val-Gly) polymer indicate an elastomeric mechanical response in which the elastic modulus does value in comparison to the (Val-Pro-Gly-Val-Gly) polymer. These smdies of glycine suhstitution support the hypothesis that type-II p-tum formation can he associated with the development of elastomeric behavior with native elastins and elastin-derived polypeptide sequences. Several investigators have proposed that the (Val-Pro-Gly-Val-Gly) pentapeptide represents the minimal viscoelastic unit... 

Beyond the elastic modulus, SFM-based colloidal probe measuronents were successfully applied to study interaction forces between thermo-responsive polymers and protein-coated surfaces. This was shown by Cole, Voelcker, Thissen, Horn, and Griesser (2010) with bovine serum albumin-coated probes on PNiPAAm surfaces. Furthermore, time-dependent colloidal probe measuronents on thermo-responsive polymer coatings... 

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