Silk-elastin-like proteins

Silk. Structural studies of the model peptides of Bombyx mori silk-elastin like protein were undertaken using solid state NMR. Detailed structural analyses were performed using deconvolution subroutines assuming Gaussian line shapes for the Ala peaks. 

Nagarsekar, A., Crissman, J., Crissman, M. et al. (2002) Genetic synthesis and characterization of pH-and temperature-sensitive silk-elastin-like protein block copolymers. Journal of Biomedical Materials Research, 62,195-203. 

Dandu, R., Von Cresce, A., Briber, R. et al. (2009) Silk-elastin-like protein polymer hydrogels Influence of monomer sequence on physicochemical properties. Polymer, 50, 366-374. 

Hatefi, A., Cappello, J. and Ghandehari, H. (2007) Adenoviral gene delivery to solid tumors by recombinant silk-elastin-like protein polymers. Pharmaceutical Research, 24,773-779. 

Cresce, A. V., Dandu, R., Burger, A. et al. (2008) Characterization and real-time imaging of gene expression of adenovirus embedded silk-elastin-like protein polymer hydrogels. Molecular Pharmaceutics, 5, 891-897. 

Ehnerman, A.A., CappeUo, J., Ghandehari, H. and Hoag, S.W. (2002) Solute diffusion in genetically engineered silk-elastin-like protein polymer hydrogels. Journal of Controlled Release, 82,277-287. 

Ner, Y., Stuart, J.A., Whited, G. and Sotzing, G.A. (2009) Electrospinning nanoribbons of a bioengineered silk-elastin-like protein (SELF) from water. Polymer, 50, 5828-5836. 

Qiu, W, CappeUo, J. and Wu, X. (2011) Autoclaving as a chemical-free process to stabilize recombinant silk-elastin-like protein polymer nanofibers. Applied Physics Letters, 98, doi 10.1063/1.3604786... 

Price, R., Gustafson, J., Greish, K. et al. (2012) Comparison of silk-elastin-like protein polymer hydrogel and poloxamer in matrix-mediated gene deUvery. International Journal of Pharmaceutics, 427, 97-104. 

Collins, T., Azevedo-SUva, J., da Costa, A., Branca, F., Machado, R. and Casal, M. (2013) Batch production of a silk-elastin-like protein in E. coli BL21(DE3) key parameters for optimisation. Microbial Cell Factories, 12, 21. 

VPGIG)2VPGKG[Pg.3527]

Qiu WG, Teng WB, Cappello JY, Wu X (2009) Wet-spinning of recombinant silk-elastin-like protein polymer fibers with high tensile strength and high deformability. Biomacromolecules 10 602-608... 

A particular kind of materials are the silk-elastin-like protein polymers (SELPs), consisting of the repeating units of silk and elastin blocks, which combine a set of outstanding physical and biological properties of silk and elastin. SELPs can undergo tunable... 

Future Trends for Recombinant Protein-Based Polymers The Case Study of Development and Application of Silk-Elastin-Like... 

This overview will mainly focus on those polymers found in natural structural proteins, particularly the silk-elastin-like polymers (SELPs) of recombinant DNA technology origin. 

Resilin and elastin have relatively high extensibility and resilience, but as compared to the collagen and the silks, the proteins sacrifice stiffness (elastic modulus) and strength (see Table 2). Collagen and dragUne sflk are much stiffer materials, but lack the extensibility that is characteristic of the rubber-like proteins. On the other hand, the mussel byssus fibers and the viscid silk have the extensibility of resilin and elastin, but lack the resilience [208]. 

Some polymers have been purified on the basis of their physicochemical properties. For example, silk-like polymers have been purified by taking advantage of their low solubility in aqueous medium (13). Elastin-like polymers (ELPs) have been purified by temperature cycling above and below their inverse temperature transition (Tt) (14). This technique has been extended to produce an ELP-tag that can be used to purify a number of recombinant proteins by temperature cycling, which may be faster and less expensive than affinity chromatography (15). 

Historically, these peptides were identified by isolating domains of interest from naturally evolved proteins. The tripeptide RGD sequence (arginine-glycine-aspartic acid), a commonly used cell-adhesion domain, is a prime example of this. RGD was isolated in 1983 from the extracellular and plasma protein fibronectin and was identified as the minimal sequence necessary to promote cell-attachment properties (Pierschbacher and Ruoslahti 1984). Other commonly used domains include elastin-like sequences, which are derived from the protein elastin found in connective tissue (Meyer and ChiUcoti 2002), and recombinant-silks (Prince et al. 1995). Both of these peptide domains are used to confer their unique mechanical properties (i.e., resilience, elasticity, and strength) to the resulting biomaterial. 

---