Difference between revisions of "Part:BBa K1919000"

Revision as of 15:30, 11 October 2016

The coding sequence of antimicrobial peptide CecropinXJ

Antimicrobial peptide CecropinXJ belongs to AMP family Cecropin, a group of small basic polypeptides mainly found in the hemolymph of insects, consist of 31-39 amino acid residues and have a broad spectrum, high heat stability and potent bacteriostatic activity.

Sequence and Features

Usage and Biology

Antimicrobial peptides (AMPs) are a group of peptides that play roles in the innate immune system to protect the host from invading pathogens [1]. AMPs have minimal toxicity and low sensitivity effects to the host [2], which means antimicrobial peptides have the potential to be used to replace antibiotics in the future. Thus, the detrimental effects of antibiotics overuse will be released.

Cecropins, a group of small AMPs mainly found in the hemolymph of insects, consist of 31 39 amino acid residues and have a broad spectrum, high heat stability and potent bacteriostatic activity [3-5]. CecropinXJ (Part BBa_K1919000) is a member of the Cecropin family, which was first cloned from the larvae of the Xinjiang silkworm (Bombyx mori). Previous researches have determined the complete amino acid sequence of this molecule [6]. It has been demonstrated that CecropinXJ could be expressed in eukaryotic expression system such as Pichia pastoris [7] or prokaryotic expression system such as E.coli [8]. What’s more, CecropinXJ exhibited to have various activities such as antibacterial activity against both Gram‑positive and Gram-negative bacteria, as well as antifungal activity [8]. These characteristics indicate that CecropinXJ is an ideal antimicrobial substance to be used to treat foot diseases caused by microbes.

In recent years, studies concerning the expression of anti¬microbial peptides have mainly focused on the use of fusion partners [9]. For example, Thioredoxin, a heat-stable and low molecular weight soluble protein in the prokaryotic cytoplasm, has been shown to display chaperone like activity [10]. Fusion proteins of antimicrobial peptides generated in E. coli reduce the toxic effect of antimicrobial peptides to the host cells and protect the small antimicrobial peptides from proteolytic degradation.

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