Difference between revisions of "Part:BBa K2309025:Design"

 
(→‎References)
 
(One intermediate revision by the same user not shown)
Line 7: Line 7:
  
 
===Design Notes===
 
===Design Notes===
−
blackbass genomic DNA
+
Grammistins are a group of peptides secreted by soapfishes and characterized by its amphiphilic -helical structure. There are four types of Grammistins: Pp1,Pp3, Gs1, and Gs2. Gs 1 and Gs 2 are from Grammistes sexlineatus and Pp 1 and Pp 3 from Pogonoperca punctata (Yokota, Nagashima, and Shiom, 2001). Grammistin-Pp1 is made up of thirteen amino acid residues. Studies showed that Grammistin-Pp1 could interact with phospholipids and influence the permeability of membrane. Sugiyama et al. (2006) reported that the peptide Grammistin-Pp1 is effective on both Gram negative bacteria and Gram positive bacteria, which includes Staphylococcus aureus.
−
 
+
−
 
+
  
 
===Source===
 
===Source===
Line 16: Line 14:
  
 
===References===
 
===References===
 +
Yokota, H., Nagashima, Y., and Shiom, K., (2001) ‘Interaction of grammistins with lipids and their antibacterial activity’, Fisheries Science, 2001 (67), pp. 928-933, ScienceDirect [Online]. Available from: http://www.sciencedirect.com (Accessed: 2017 August 26th)
 +
 +
Sugiyama, N. et al. (2006) ‘Biological activities of synthetic grammistins and analogous peptides’, Fisheries Science, 2006 (72), pp. 1114-1120, ScienceDirect [Online]. Available from: http://www.sciencedirect.com(Accessed: 2017 August 26th)

Latest revision as of 08:29, 1 November 2017


Grammistin-Pp1 for Lactococcus lactis NZ9000 (codon optimized)


Assembly Compatibility:
  • 10
    COMPATIBLE WITH RFC[10]
  • 12
    COMPATIBLE WITH RFC[12]
  • 21
    COMPATIBLE WITH RFC[21]
  • 23
    COMPATIBLE WITH RFC[23]
  • 25
    COMPATIBLE WITH RFC[25]
  • 1000
    COMPATIBLE WITH RFC[1000]


Design Notes

Grammistins are a group of peptides secreted by soapfishes and characterized by its amphiphilic -helical structure. There are four types of Grammistins: Pp1,Pp3, Gs1, and Gs2. Gs 1 and Gs 2 are from Grammistes sexlineatus and Pp 1 and Pp 3 from Pogonoperca punctata (Yokota, Nagashima, and Shiom, 2001). Grammistin-Pp1 is made up of thirteen amino acid residues. Studies showed that Grammistin-Pp1 could interact with phospholipids and influence the permeability of membrane. Sugiyama et al. (2006) reported that the peptide Grammistin-Pp1 is effective on both Gram negative bacteria and Gram positive bacteria, which includes Staphylococcus aureus.

Source

This part is optimized from part BBa_K1162003. The original part BBa_K1162003, actually, is suitable for Escherichia coli. This part has optimized codon usage which applicable to Lactococcus lactis NZ9000 strain

References

Yokota, H., Nagashima, Y., and Shiom, K., (2001) ‘Interaction of grammistins with lipids and their antibacterial activity’, Fisheries Science, 2001 (67), pp. 928-933, ScienceDirect [Online]. Available from: http://www.sciencedirect.com (Accessed: 2017 August 26th)

Sugiyama, N. et al. (2006) ‘Biological activities of synthetic grammistins and analogous peptides’, Fisheries Science, 2006 (72), pp. 1114-1120, ScienceDirect [Online]. Available from: http://www.sciencedirect.com(Accessed: 2017 August 26th)