Elastin polypeptides

Keeley, F.W., Bellingham, C.M., and Woodhouse, K.A., Elastin as a self-organising biomaterial Use of recombinantly expressed human elastin polypeptides as a model system for investigations of structure and self-assembly of elastin, Philos. Trans. R. Soc. Lond. B Biol. Sci., 357, 185-189, 2002. 

Belhngham, C.M., Lillie, M.A., Gosline, J.M., Wright, G.M., Starcher, B.C., Bailey, A.J., Woodhouse, K.A., and Keeley, F.W., Recombinant human elastin polypeptides self-assemble into biomaterials with elastin-hke... 

A feature of mature elastin is the presence of covalent cross-links that connect elastin polypeptide chains into a fiber network. The major cross-linkages involve desmo-sine and isodesmosine, both of which are derived from lysine residues. Several regions rich in lysine residues can provide cross-links. Two such regions that contain peptide sequences that are repeated several times in tropoelastin have the primary structure -Lys-Ala-Ala-Ala-Lys- and... 

Bellingham CM, Woodhouse KA, Robson P, et al. Self-aggregation characteristics of re-combinantly expressed human elastin polypeptides. Biochim. Biophys. Acta, 2001 1550(1) 6-19. 

Woodhouse KA, Klement P, Chen V, et al. Investigation of recombinant human elastin polypeptides as non-thrombogenic coatings. Biomaterials, 2004 25(19) 4543-4553. 

Figure 3 (a) Comparison of the turbidimetric profiles for a series of chemosynthetic elastin polypeptides based on random copolymers of the repeat sequence [(Val-Pro-Gly-Val-Gly)i x(Val-Pro-Gly-Xaa-Gly)J, where fx refers to the mole fraction of variant pentapeptides within the polymer sequence. " (b) Hydrophobicity scale based on ft values for the copolymers described above as a function of guest residue identity and mole fraction, f. Note that hydrophobic amino acids shift the position of 7 toward lower temperature and that more polar guest residues shift the position of 7i toward higher temperatures in a manner commensurate with the level of substitution within the polypeptide sequence. Reprinted from Uriy, D. W. Gowda, D. C. Parker, T. M. etal. Biopolymers 99Z, 32(9), 1243 20(b) Copyright 1992, with permission from Wiley. 

Figm 13 (a) Sequence and schematic representation of the self-assembly of an amphiphilic diblock elastin polypeptide into core-shell nanoparticles. Elastin-mimetic protein polymers that comprise fusions of elastin sequences with different 7, values can be induced to undergo self-assembly at a temperature between the two transition temperatures, (b) Differential scanning calorimetry measurements indicate an endothermic transition for the more hydrophobic (lower 7 block with a value that corresponds to those observed for the burial of hydro-phobic residues within a folded protein, (c) This transition coincides with the formation of spherical assemblies in which the more hydrophobic block is confined within the micellar core. Transmission electron microscopy measurements are consistent with spherical micelles and more complex assemblies. Reprinted from Lee, T. A. T. Cooper, A. Apkarian, R. P. Conticello, V. P. Adv. Mater. 2000, f2(15), Copyright 2000, with... 

K.A. Woodhouse, P. Klement, V. Chen, M.B. Gorbet, F.W. Keeley, R. Stahl, J.D. Fromstein, C.M. Bellingham, Investigation of recombinant human elastin polypeptides as non-thrombogenic coatings. Biomaterials 25(19), 4543-4553 (2004)... 

Bellingham, C. M., M. A. Lillie, J. M. GosUne, G. M. Wright, B. C. Starcher, A. J. Bailey, K. A. Woodhouse, and F. W. Keeley. 2003. Recombinant human elastin polypeptides self-assemble into biomaterials with elastin-like properties. Biopolymers 70(4) 445-55. 

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