Literature DB >> 11061996

High-level expression of antimicrobial peptide mediated by a fusion partner reinforcing formation of inclusion bodies.

J H Lee1, J H Kim, S W Hwang, W J Lee, H K Yoon, H S Lee, S S Hong.   

Abstract

A gene expression system for antimicrobial peptides, which could be effectively used for various studies or applications of the antimicrobial peptides, has been developed. To avoid the harmful effects on an expression host, Escherichia coli, the antimicrobial peptides were expressed as fusion proteins with a polypeptide F4, which is a truncated PurF fragment that highly tends to form inclusion bodies. Seven different kinds of antimicrobial peptides have been successfully expressed by this expression system and the resulting expression level of fusion proteins reached up to 30% of total cell proteins. To confirm the identity of the recombinant peptide, MSI-344 was selected as a model peptide and purified to homogeneity, and we could obtain the recombinant MSI-344 of a high purity and with a good yield, which was identical to the authentic peptide in the aspects of the chemical and antimicrobial properties. These results show that the neutral fusion partner, which reinforces the formation of inclusion bodies, could mediate a high-level expression of the antimicrobial peptides. Copyright 2000 Academic Press.

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Year:  2000        PMID: 11061996     DOI: 10.1006/bbrc.2000.3712

Source DB:  PubMed          Journal:  Biochem Biophys Res Commun        ISSN: 0006-291X            Impact factor:   3.575


  19 in total

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4.  Powerful workhorses for antimicrobial peptide expression and characterization.

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5.  Design, characterization and expression of a novel hybrid peptides melittin (1-13)-LL37 (17-30).

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Review 6.  Synthetic Biology and Computer-Based Frameworks for Antimicrobial Peptide Discovery.

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Journal:  ACS Nano       Date:  2021-02-04       Impact factor: 15.881

7.  Recombinant Tandem Repeated Expression of S3 and SΔ3 Antimicrobial Peptides.

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8.  A novel PCR-based method for high throughput prokaryotic expression of antimicrobial peptide genes.

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9.  Expression of porcine protegrin-1 in Pichia pastoris and its anticancer activity in vitro.

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10.  Preparation of Specific Polyclonal Antibody Against the Recombinant Mutacin Produced by sfGFP Fusion Protein Technology.

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Journal:  Open Microbiol J       Date:  2015-07-31
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