IGEM:IMPERIAL/2008/Bioprinter/Subteam 3: Difference between revisions
| Line 9: | Line 9: | ||
Hydrophobic domains are rich in glycine, valine, proline and other non-polar amino acids, often present in tandem peptide repeats. Crosslinking domains are rich in alanine and contain lysine residues, which form covalent crosslinks that stabilise the polymeric form of elastin. | Hydrophobic domains are rich in glycine, valine, proline and other non-polar amino acids, often present in tandem peptide repeats. Crosslinking domains are rich in alanine and contain lysine residues, which form covalent crosslinks that stabilise the polymeric form of elastin. | ||
Under appropriate conditions of temperature and ionic strength, elastin undergoes a self-aggregation process called coacervation, in which the protein separate from solution as a second phase. Coacervation is usually induced by an increase in temperature. Unlike most proteins which undergo denaturation with increased temperature in solution, elastin polypeptides become more ordered through coacervation. The temperature at which coacervation occurs is dependent on ionic strength, pH, protein concentration and relative proportions of hydrophobic and hydrophilic residues in synthetic polypeptides. | |||
== EAK16-II == | == EAK16-II == | ||
Revision as of 01:37, 25 July 2008
Biomaterials
We aim to synthesize two types of biomaterials, elastin and EAK16-II 3D scaffolds.
Elastin
Elastin is a polymeric extracellular matrix protein found in tissues requiring extensibility and elastic recoil, including arteries, lungs, ligaments and skin. The precursor for elastin is a soluble protein called tropoelastin. The sequence of tropoelastin consists of alternating hydrophobic and crosslinking domains, with distinct exons coding each domain.
Hydrophobic domains are rich in glycine, valine, proline and other non-polar amino acids, often present in tandem peptide repeats. Crosslinking domains are rich in alanine and contain lysine residues, which form covalent crosslinks that stabilise the polymeric form of elastin.
Under appropriate conditions of temperature and ionic strength, elastin undergoes a self-aggregation process called coacervation, in which the protein separate from solution as a second phase. Coacervation is usually induced by an increase in temperature. Unlike most proteins which undergo denaturation with increased temperature in solution, elastin polypeptides become more ordered through coacervation. The temperature at which coacervation occurs is dependent on ionic strength, pH, protein concentration and relative proportions of hydrophobic and hydrophilic residues in synthetic polypeptides.
EAK16-II
AEAEAKAKAEAEAKAK
Signalling Peptides
SacB: MNIKKFAKQATVLTFTTALLAGGATQAFAKET
LipA: MKFVKRRIIALVTILMLSVTSLFALQPSAKAAEH
Epr: MKNMSCKLVVSVTLFFSFLTIGPLAHAQNS
