BIOT 267 |
| Endotoxins (or lipopolysaccharide complexes) are fragments of outer wall of Gram-negative bacteria which are released during normal cell metabolism and the death of Gram-negative cells. Endotoxin infection can lead to a simple fever up to multi-organs failure associated with sepsis. It has been reported that sepsis has caused 10-15% of children mortality rate and up to 40% in adults. Sterilization, such as autoclaving or sterile filtration which is normally practiced in pharmaceutical and medical industries, barely has effect on removing endotoxin. Therefore, simple, cost-effective and fast removal of endotoxin still persists as a problem in food, water resources, medical, pharmaceutical and microelectronics industries. The Sushi3 domain (a peptide consists of 34 amino acids), isolated from the horseshoe crab, exhibits exceptionally high binding affinity with endotoxin. Even though the Sushi 3 has been expressed in E. coli, but the purification steps are very complicated, costly and time-consuming, which is not suitable for mass-production and large-scale removal/neutralization of endotoxin. A peptide can also be synthesized by chemical method, but it is very expensive to synthesize 34-amino acid Sushi3 peptide. So there is an urgent need to develop a new, simple, fast and cost-effective method for mass-production of such peptide in order to achieve large-scale neutralization/removal of endotoxin. In this project, we will use DNA recombinant technology to construct the gene coding for the polypeptide fusion of elastin like polymer-Sushi3 and perform the thermally-triggered purification, and achieve the simple and cost-effective mass-production of Sushi 3. Large-scale neutralization/removal of endotoxin will also be investigated in this project. |
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Poster Session
5:30 PM-7:30 PM, Wednesday, August 22, 2007 BCEC -- Exhibit Hall - B2, Poster
Division of Biochemical Technology |