Resilin-like polypeptides

Lyons, R.E., Lesieur, E., Kim, M., Wong, D., Brownlee, A., Pearson, R., and Elvin, C., The development of synthetic genes encoding repetitive resilin-like polypeptides Construct design, bacterial expression and rapid purification. Protein Eng. Design Select., 20(1), 25-32, 2007. 

Keywords Elastin Elastin-like polypeptides Elastomeric polypeptides Resilin Resilin-like polypeptides... 

This chapter will discuss the basic aspects of elastin and resilin and will address their biological role, biochemical processing, and properties. The materials inspired by elastin and resilin, such as elastin-like polypeptides and resilin-like polypeptides, and applications thereof, will also be covered. 

Table 4 Secondary structure analysis a comparison of resilin-like polypeptides...

Resilin-like polypeptide and sequence motif Technique Helices (%) Strands (%) Turns (%) Unordered (%) (or random coil) Beta sheet (%) PPII (%)... 

Interestingly, the CD of Drosl6 demonstrated a more ordered protein with more p-structure than the other two resilin-like polypeptides [229]. 

Multiple applications for resilin-like polypeptides have garnered renewed research interest since the report of the first recombinant resilin in 2005. The excellent mechanical properties of the resilin-like polypeptides has directed investigation toward their use as high-performance materials and in tissue engineering applications. It is widely acknowledged that cells interact and take cues from their microenvironment and, therefore, the development of polymeric scaffolds to mimic the extracellular matrix and drive desired cell or tissue responses has been of wide interest. To this end, our laboratories have developed a modular resilin-like polypeptide (RLP12) (see Fig. 20) that contains not only twelve repeats of the... 

Fig. 20 Modular resilin-like polypeptide containing domains conferring elastomeric properties, heparin molecule interaction, cell adhesion, and matrix metalloproteinase (MMP) proteolysis. Lysine residues are encoded periodically to permit crosslinking...

As shown in Table 3, in aqueous solution these short resilin-like peptides adopt a mixture of PPII stmcture, unordered conformations, and p-tums, while in Ttifluoroethanol (TFE) primarily type-11 p tums populate the conformational space. These findings are consistent with what Andersen has predicted and are also very similar to other elastomeric proteins studied. Interestingly, coacervation, a common phenomenon in elastin and abductin (in which a protein-rich phase is formed when the temperature is raised), has not been observed in resilin-like polypeptides (RLPs). This is almost certainly due to the inaeased hydrophilicity of resilin, which is soluble in water under all relevant experimental conditions. As mentioned above, additional spectroscopic studies on extended RLPs, as well as manipulations of RLP sequences via the introduction of different amino acid analogs and evaluation of corresponding conformational changes, would be useful to elucidate the mechanism of elasticity of resilin. 

Resilin a Structural protein (see) from the exoskeleton of arthropods, espedally insects. R. has a high glydne content, and no cystine. It is located between the chitin lamellae, and endows the arthropod exoskeleton with a certain elasticity. A notable component of R. is trityrosine (Fig.), which is formed (after translation of the protein) by cross linking the tyrosine side chains of one or more polypeptide chains. This results in an irregular three dimensional lattice, which is responsible for the rubber-like properties of R. 

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