Next Article in Journal
Exploration of Scaffolds from Natural Products with Antiplasmodial Activities, Currently Registered Antimalarial Drugs and Public Malarial Screen Data
Previous Article in Journal
Synthesis of Canthardin Sulfanilamides and Their Acid Anhydride Analogues via a Ring-Opening Reaction of Activated Aziridines and Their Associated Pharmacological Effects
Article Menu
Issue 1 (January) cover image

Export Article

Open AccessArticle
Molecules 2016, 21(1), 103; doi:10.3390/molecules21010103

Antibacterial Peptide CecropinB2 Production via Various Host and Construct Systems

1
Department of Chemical Engineering, National Chung Hsing University, 250 Kuo Kuang Road, Taichung 40227, Taiwan
2
Biotechnology Center, National Chung Hsing University, 250 Kuo Kuang Road, Taichung 40227, Taiwan
*
Author to whom correspondence should be addressed.
Academic Editors: Fernando Albericio and Derek J. McPhee
Received: 7 December 2015 / Revised: 5 January 2016 / Accepted: 13 January 2016 / Published: 16 January 2016
(This article belongs to the Section Medicinal Chemistry)
View Full-Text   |   Download PDF [1244 KB, uploaded 16 January 2016]   |  

Abstract

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. View Full-Text
Keywords: cecropinB2; antibacterial peptides; multi-drug-resistant; Pichia pastoris; Bacillus subtilis cecropinB2; antibacterial peptides; multi-drug-resistant; Pichia pastoris; Bacillus subtilis
Figures

Figure 1a

This is an open access article distributed under the Creative Commons Attribution License which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited. (CC BY 4.0).

Scifeed alert for new publications

Never miss any articles matching your research from any publisher
  • Get alerts for new papers matching your research
  • Find out the new papers from selected authors
  • Updated daily for 49'000+ journals and 6000+ publishers
  • Define your Scifeed now

SciFeed Share & Cite This Article

MDPI and ACS Style

Lai, W.-S.; Kan, S.-C.; Lin, C.-C.; Shieh, C.-J.; Liu, Y.-C. Antibacterial Peptide CecropinB2 Production via Various Host and Construct Systems. Molecules 2016, 21, 103.

Show more citation formats Show less citations formats

Note that from the first issue of 2016, MDPI journals use article numbers instead of page numbers. See further details here.

Related Articles

Article Metrics

Article Access Statistics

1

Comments

[Return to top]

Molecules EISSN 1420-3049 Published by MDPI AG, Basel, Switzerland RSS E-Mail Table of Contents Alert
Back to Top