Difference between revisions of "Part:BBa K2309021:Design"

 
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===Design Notes===
 
===Design Notes===
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Homo sapiens genomic DNA
 
  
  
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LL-37 is the only cathelicidin-derived antimicrobial peptide found in humans (Dürr, Sudheendra and Ramamoorthy, 2006). Mature LL-37 has 37 amino acid residues starting with two leucines (NH2-LLGDFFRKSKEKIGKEFKRIVQRIKDFLRNLVPRTES-COOH).The peptide is cleaved from a larger protein, hCAP-18, by extracellular proteolysis of proteinase 3 from the C-terminal end of hCAP18(Patricia, 2010; Ramos, Domingues, and Gama, 2011).The peptide is composed of two main parts: from residues Leu2 to Leu31, which is a α-helical structure(Fig 2b), and a 6 residues form the loop structure at the terminus.
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Ramos, Domingues, and Gama (2011) also reported that LL-37 has additional roles such as regulating the inflammatory response in wounds or infection sites, binding and neutralizing lipopolysaccharide (LPS), and wound closure, apart from its anti-microbial property.
  
 
===Source===
 
===Source===
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===References===
 
===References===
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Samperio.P (2010) ‘The human cathelicidin hCAP18/LL-37: A multifunctional peptide involved inmycobacterial infections’, Peptides, 31 (2010), pp. 1791-1798, ScienceDirect [Online]. DOI: 10.1016/j.peptides.2010.06.016 (Accessed: 2017 August 28th)
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Ramos. R., Domingues. L., Gama. M., (2011) ‘LL37, a human antimicrobial peptide with immunomodulatory properties’, Science against microbial pathogens: communicating current research and technological advances, pp. 915-925, ScienceDirect [Online].Available from: www.sciencedirect.com (Accessed: 2017 August 24th)
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Dürr. U., Sudheendra. U., Ramamoorthy. A., (2006) ‘Review LL-37, the only human member of the cathelicidin family of antimicrobial peptides’, Biochimica et Biophysica Acta, 1758 (2006), pp. 1408–1425, ScienceDirect [Online]. DOI: 10.1016/j.bbamem.2006.03.030 (Accessed: 2017 August 24th)

Latest revision as of 08:21, 1 November 2017


LL-37 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

LL-37 is the only cathelicidin-derived antimicrobial peptide found in humans (Dürr, Sudheendra and Ramamoorthy, 2006). Mature LL-37 has 37 amino acid residues starting with two leucines (NH2-LLGDFFRKSKEKIGKEFKRIVQRIKDFLRNLVPRTES-COOH).The peptide is cleaved from a larger protein, hCAP-18, by extracellular proteolysis of proteinase 3 from the C-terminal end of hCAP18(Patricia, 2010; Ramos, Domingues, and Gama, 2011).The peptide is composed of two main parts: from residues Leu2 to Leu31, which is a α-helical structure(Fig 2b), and a 6 residues form the loop structure at the terminus. Ramos, Domingues, and Gama (2011) also reported that LL-37 has additional roles such as regulating the inflammatory response in wounds or infection sites, binding and neutralizing lipopolysaccharide (LPS), and wound closure, apart from its anti-microbial property.

Source

This part is optimized from part BBa_K1162006. The original part BBa_K1162006, actually, is suitable for Escherichia coli. This part has optimized codon usage which applicable to Lactococcus lactis NZ9000 strain

References

Samperio.P (2010) ‘The human cathelicidin hCAP18/LL-37: A multifunctional peptide involved inmycobacterial infections’, Peptides, 31 (2010), pp. 1791-1798, ScienceDirect [Online]. DOI: 10.1016/j.peptides.2010.06.016 (Accessed: 2017 August 28th)

Ramos. R., Domingues. L., Gama. M., (2011) ‘LL37, a human antimicrobial peptide with immunomodulatory properties’, Science against microbial pathogens: communicating current research and technological advances, pp. 915-925, ScienceDirect [Online].Available from: www.sciencedirect.com (Accessed: 2017 August 24th)

Dürr. U., Sudheendra. U., Ramamoorthy. A., (2006) ‘Review LL-37, the only human member of the cathelicidin family of antimicrobial peptides’, Biochimica et Biophysica Acta, 1758 (2006), pp. 1408–1425, ScienceDirect [Online]. DOI: 10.1016/j.bbamem.2006.03.030 (Accessed: 2017 August 24th)