Antibacterial Peptide CecropinB2 Production via Various Host and Construct Systems
| Autor: | Chia-Chi Lin, Wei-Shiang Lai, Shu-Chen Kan, Yung-Chuan Liu, Chwen-Jen Shieh |
|---|---|
| Jazyk: | angličtina |
| Rok vydání: | 2016 |
| Předmět: |
0301 basic medicine
Signal peptide Acinetobacter baumannii Recombinant Fusion Proteins Genetic Vectors Pharmaceutical Science Gene Expression Peptide Bacillus subtilis Microbial Sensitivity Tests Biology Protein Sorting Signals medicine.disease_cause Protein Engineering Article Pichia Analytical Chemistry Pichia pastoris Microbiology Inteins lcsh:QD241-441 03 medical and health sciences cecropinB2 lcsh:Organic chemistry Drug Discovery medicine Escherichia coli Physical and Theoretical Chemistry antibacterial peptides multi-drug-resistant chemistry.chemical_classification Organic Chemistry biology.organism_classification 030104 developmental biology Cecropin chemistry Chemistry (miscellaneous) Molecular Medicine Insect Proteins Antibacterial activity Antimicrobial Cationic Peptides Plasmids |
| Zdroj: | Molecules Molecules; Volume 21; Issue 1; Pages: 103 Molecules, Vol 21, Iss 1, p 103 (2016) |
| ISSN: | 1420-3049 |
| Popis: | Cecropin is a cationic antibacterial peptide composed of 35–39 residues. This peptide has been identified as possessing strong antibacterial activity and low toxicity against eukaryotic cells, and it has been claimed that some types of the cecropin family of peptides are capable of killing cancer cells. In this study, the host effect of cloning antibacterial peptide cecropinB2 was investigated. Three different host expression systems were chosen, i.e., Escherichia coli, Bacillus subtilis and Pichia pastoris. Two gene constructs, cecropinB2 (cecB2) and intein-cecropinB2 (INT-cecB2), were applied. Signal peptide and propeptide from Armigeres subalbatus were also attached to the gene construct. The results showed that the best host for cloning cecropinB2 was P. pastoris SMD1168 harboring the gene of pGAPzαC-prepro-cecB2 via Western blot confirmation. The cecropinB2 that was purified using immobilized-metal affinity chromatography resin showed strong antibacterial activity against the Gram-negative strains, including the multi-drug-resistant bacteria Acinetobacter baumannii. |
| Databáze: | OpenAIRE |
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