Difference between revisions of "Team:HokkaidoU Japan/co-expression"
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If we need antimicrobial peptides (AMPs), we usually get it from chemical synthesis method because its amino acid residues are less than another peptide. However chemical synthesis method is unsuitable for the case which a large amount of isotopically labeled peptides is essential for structural study by NMR. In this case, we’ll choose the recombinant synthesis method but, of course, AMPs are harmful to host bacteria. To prevent host toxicity, there is the solution which utilizes expression with inclusion bodies. In addition, in case that it is not promising to form inclusion bodies, we make a partner protein which has the high potential to form inclusion bodies co-express with protein of interest. | If we need antimicrobial peptides (AMPs), we usually get it from chemical synthesis method because its amino acid residues are less than another peptide. However chemical synthesis method is unsuitable for the case which a large amount of isotopically labeled peptides is essential for structural study by NMR. In this case, we’ll choose the recombinant synthesis method but, of course, AMPs are harmful to host bacteria. To prevent host toxicity, there is the solution which utilizes expression with inclusion bodies. In addition, in case that it is not promising to form inclusion bodies, we make a partner protein which has the high potential to form inclusion bodies co-express with protein of interest. | ||
| − | + | <h3 id="abf-2">ABF-2</h3> | |
ABF-2 is one of the AMPs derived from Caenorhabditis elegans. ABF-2 belongs to the CSαβ superfamily which has both α-helix and antiparallel β-sheet stabilized by some disulfide bonds and interacts to cell membrane like thanatin. It is difficult for ABF-2 to form inclusion bodies alone. So the recombinant synthesis method by co-expression system may be effectible. | ABF-2 is one of the AMPs derived from Caenorhabditis elegans. ABF-2 belongs to the CSαβ superfamily which has both α-helix and antiparallel β-sheet stabilized by some disulfide bonds and interacts to cell membrane like thanatin. It is difficult for ABF-2 to form inclusion bodies alone. So the recombinant synthesis method by co-expression system may be effectible. | ||
Revision as of 16:24, 14 September 2015
Co-expression System
Overview
If we need antimicrobial peptides (AMPs), we usually get it from chemical synthesis method because its amino acid residues are less than another peptide. However chemical synthesis method is unsuitable for the case which a large amount of isotopically labeled peptides is essential for structural study by NMR. In this case, we’ll choose the recombinant synthesis method but, of course, AMPs are harmful to host bacteria. To prevent host toxicity, there is the solution which utilizes expression with inclusion bodies. In addition, in case that it is not promising to form inclusion bodies, we make a partner protein which has the high potential to form inclusion bodies co-express with protein of interest.ABF-2
ABF-2 is one of the AMPs derived from Caenorhabditis elegans. ABF-2 belongs to the CSαβ superfamily which has both α-helix and antiparallel β-sheet stabilized by some disulfide bonds and interacts to cell membrane like thanatin. It is difficult for ABF-2 to form inclusion bodies alone. So the recombinant synthesis method by co-expression system may be effectible.Design
Experiments
Result
Conclusion
