Elastin-like peptide

Reiersen H, Clarke AR, Rees AR (1998) Short elastin-like peptides exhibit the same temperature-induced structural transitions as elastin polymers implications for protein engineering. J Mol Biol 283 255-264... 

The formation of spanning H-bonded water networks on the surface of biomolecules has been connected with the widely accepted view that a certain amount of hydration water is necessary for the dynamics and function of proteins. Its percolative nature had been suggested first by Careri et al. (59) on the basis of proton conductivity measurements on lysozyme this hypothesis was later supported by extensive computer simulations on the hydration of proteins like lysozyme and SNase, elastine like peptides, and DNA fragments (53). The extremely interesting... 

Yang G, Woodhouse KA, Yip CM. Substrate-facilitated assembly of elastin-like peptides studies by variable-temperature in situ atomic force microscopy. J. Am. Chem. Soc.,... 

Jia and coworkers took advantage of CuAAC to design an elastin-like peptide-polymer conjugate. The reaction between a bifunctional, azide-terminated PEO block and an alkyne-functionalized peptide composed of two different functional domains yielded a multiblock copolymer (Figure 1.12). 

Elastin like peptide Hexafluoroisopropanol Lipopolysaccharides Major ampullate spidroin Spiders... 

Finally, temperature-sensitive, elastin-like peptide-modified dendrimers were synthesized for drug delivery by Kojima et al. [ 140]. Elastin is one of the major components of the extracellular matrix with temperature sensitivity. A repeat sequence of Val-Pro-Gly-Val-Gly was used to prepare the elastin-like peptide, which was conjugated to a PAMAM dendrimer G(4). The synthesized elastin-mimetic dendrimer-based polymer proved to be a potent drug carrier with both temperature- and pH-responsive properties. The same group reported fine-tuning of the temperature sensitivity by manipulation of the peptide chain length and the generation of dendrimer. 

Coacervation occurs in tropoelastin solutions and is a precursor event in the assembly of elastin nanofibrils [42]. This phenomenon is thought to be mainly due to the interaction between hydro-phobic domains of tropoelastin. In scanning electron microscopy (SEM) picmres, nanofibril stmc-tures are visible in coacervate solutions of elastin-based peptides [37,43]. Indeed, Wright et al. [44] describe the self-association characteristics of multidomain proteins containing near-identical peptide repeat motifs. They suggest that this form of self-assembly occurs via specific intermolecular association, based on the repetition of identical or near-identical amino acid sequences. This specificity is consistent with the principle that ordered molecular assembhes are usually more stable than disordered ones, and with the idea that native-like interactions may be generally more favorable than nonnative ones in protein aggregates. 

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. 

Elastin-like polypeptides (ELPs) are another class of synthetic biopolymers that consist of a repeating pentapeptide sequence that is represented in native elastin. The peptide sequence in ELPs is VPGXG, where X is any amino acid, except proline. ELPs are water soluble and can form micron- or sub-micron-sized aggregates moreover, they are biocompatible and nonimmunogenic, which in turn make it useful as a potent drug delivery system. ... 

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. 

Massodi I, Bidwell GL, Raucher D (2005) Evaluation of cell penetrating peptides fused to elastin-like polypeptide for drug delivery. J Controlled Release 108 396-408... 

Massodi 1, Thomas E, Rancher D (2009) Application of thermally responsive elastin-like polypeptide fused to a lactoferrin-derived peptide for treatment of pancreatic cancer. Molecules 14 1999-2015... 

Hollow capsules can be also produced with marine origin biopolymers following a layer-by-layer strategy onto a sacrificial template, as is the case of capsules formed by hyaluronic acid with polyallylamine (Szarpak et al 2008). Equivalent strategy has been also used to develop capsules with chitosan and elastin-like recombinamers (Costa et al., 2014). These capsules feature peptide sequences in their surface, bioactive RGD or nonfunctional RDG, proven to promote the viability of human mesenchymal Stan cells. Additionally, they were also able to intracellularly deliva ovalbumin, promising application with other therapeutic compounds (Costa et al., 2014). 

Elastin-like polypeptides (ELPs) have been extensively studied due to the fact that they combine similar stimulus response properties to other artificial polymers such as poly(iV-isopropylacrylamide) (pNIPAM) with the advantages of a biologically derived material, that is, it is biocompatible, modular in its composition, and can be obtained by biological processes. ELPs are polypeptides that contain a short, repetitive peptide sequence, most commonly (VPGXG) that is derived from tropoelastin, the precursor of elastin. In this sequence, X represents any amino acid sequence except proline. Polypeptides composed of the pentapeptide repeat unit VPGXG possess a reversible lower critical solution temperature (LCST). Below the LCST, the peptide is soluble... 

The elastin-derived peptide VAPG has been shown to be specific for smooth muscle cell adhesion, and PEG hydrogels modified with this adhesive peptide, rather than RGDS, support adhesion and the growth of vascular smooth muscle cells but not fibroblasts or platelets (Gobin and West., 2003). Moreover, bioactive molecules like TGF- 3 may be covalently incorporated into scaffolds to induce protein synthesis by vascular smooth muscle cells. 

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