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Elastin-derived peptides

Petersen, E., Wagberg, F., and Angquist, K. A. (2002). Serum concentrations of elastin-derived peptides in patients with specific manifestations of atherosclerotic disease. Eur. J. Vascul. Endovascul. Surg. 24, 440 444. [Pg.459]

Senior, R. M., Griffin, G. L., and Mecham, R. P. (1982). Chemotactic responses of fibroblasts to tropoelastin and elastin-derived peptides./. Clin. Invest 70, 614-618. [Pg.460]

R.M. Senior, G.L. Griffin, R.P. Mecham, Chemotactic activity of elastin-derived peptides, J. Clin. Invest. 66 (1980) 859-862. [Pg.58]

Recombinant tropoelastin and elastin-derived peptides and proteins have also been employed to investigate the mechanism of coacervation above the transition temperamre in vitro. For the recombinant human derivative SHELA26A, the coacervation process has been demonstrated to proceed in phases that depend... [Pg.78]

S. Sharpe, K. Simonetti, J. Yau, P. Walsh, Solid-state NMR characterization of auto-fluorescent fibrils formed by the elastin-derived peptide GVGVAGVG, Biomacromolecrfles 12 (2011) 1546—1555. [Pg.137]

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. [Pg.59]

Groult, V., Hornebeck, W., Ferrari, P., Tixier, J. M., Robert, L., and Jacob, M. P. (1991). Mechanisms of interaction between human skin fibroblasts and elastin Differences between elastin fibers and derived peptides. Cell Biochem. Fund. 9, 171-182. [Pg.455]

A triple helix forming collagen model peptide and a thermosensitive elastin derived pentapeptide are copolymerized using EDCCl and HOBt in DMSO. A comparison of BrCN and EDC in assembling modified DNA duplexes and DNA-RNA hybrids shows that higher yields are obtained with the slower reacting EDC. ... [Pg.263]

Massodi, E. Thomas, D. Raucher, Application of thermally responsive elastin-Uke polypeptide fused to a lactoferrin-derived peptide for treatment of pancreatic cancer. Molecules 14 (6) (2009) 1999-2015. [Pg.366]

The cyclododecaptide (Gly—Gly—L—Val—L—Pro)3 interacts with calcium with complete retention of the peptide protons upon titration with CaCl2. N-formyl and O-methyl derivatives of a-elastin act as calcifying matrices355 3S8, 359). a-elastin and insoluble elastin bind more calcium after presumably a conformational change356). [Pg.83]

Fig. 5. Structure of elastin around the ohromophoric nucleus (indicated by the circle). The nucleus links two short peptide chains together. The structure is represented as the DNP-derivative of the peptide isolated, which contains glycine (1 mole), proline (1 mole), and alanine (2 moles). One mole of alanine is A -terminal but the position of the other three amino acid residues is not known (Thomas and Partridge, 1962). Fig. 5. Structure of elastin around the ohromophoric nucleus (indicated by the circle). The nucleus links two short peptide chains together. The structure is represented as the DNP-derivative of the peptide isolated, which contains glycine (1 mole), proline (1 mole), and alanine (2 moles). One mole of alanine is A -terminal but the position of the other three amino acid residues is not known (Thomas and Partridge, 1962).
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... [Pg.180]


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See also in sourсe #XX -- [ Pg.76 ]




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