Difference between revisions of "Part:BBa K2309021"

Revision as of 08:19, 1 November 2017

LL-37 for Lactococcus lactis NZ9000 (codon optimized)

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.

Sequence and Features

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]

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 <partinfo>BBa_K2309021 short</partinfo>
-LL-37 is the most wildly used anti-microbial peptide which were exist in Homo sapiens. The structure of LL-37 can divide into two parts: alpha helix (1aa-31aa) and the loop structure (32aa-37aa) at the end.
+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.
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