Difference between revisions of "Part:BBa K2959000"

Revision as of 03:31, 28 August 2019

Expressible LL 37 - Cathelicidin

This composite part enables tha expression of the human antimicrobial peptide LL 37 in E. coli BL21 (DE3). The BioBrick consists of a T7 Promoter + RBS + LL 37 sequence + double terminator (rrnBT1 + T7TE). The T7 promoter, inducible through IPTG, controls the expression of the part.

Usage and Biology

The protein LL-37 cathelicidin is a human antimicrobial peptide active against Gram-positive bacteria, Gram-negative bacteria and fungi¹. LL-37 is the only known cathelicidin peptide produced in humans; its structure is amphipathic and has an α-helical conformation with a positive charge. Talking about its mechanism of action, the cathelicidins targeted the cell membrane and causes its complete disruption inducing cell membrane permeabilization and simultaneous vacuolar expansion. Intracellular activities of the peptide may contribute to its antifungal activity².
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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 ===Usage and Biology===
 <p align="justify">
-Defensin 1 is an antimicrobial peptide of the honeybee. It's a component of their innate immune response, which contains 51 amino acids and 6 cysteine residues forming three disulfide bonds<sup>2</sup>.  It is synthesized in salivary glands and characterizes the social immunity. Sometimes is able to protect honeybees even in early stages and act as part of individual immunity<sup>4</sup>. This AMP is expressed in the head and thorax of honey bees by the hypopharyngeal, mandibular and thoracic salivary glands<sup>3</sup>. It is present in the royal jelly, honey and hemolymph. Originally, it was isolated from royal jelly, and therefore named royalisin<sup>2</sup>.
+The protein LL-37 cathelicidin is a human antimicrobial peptide active against Gram-positive bacteria, Gram-negative bacteria and fungi<sup>1</sup>. LL-37 is the only known cathelicidin peptide produced in humans; its structure is amphipathic and has an α-helical conformation with a positive charge. Talking about its mechanism of action, the cathelicidins targeted the cell membrane and causes its complete disruption inducing cell membrane permeabilization and simultaneous vacuolar expansion. Intracellular activities of the peptide may contribute to its antifungal activity<sup>2</sup>.
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