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A simple method for the purification of an antimicrobial peptide in recombinant Escherichia coli

Hwang, Sung-Wook ; Lee, Jae-Hyun ; Park, Heung-Bok ; Pyo, Sang-Hyun LU ; So, Jin-Eon ; Lee, Hyun-Soo ; Hong, Seung-Suh and Kim, Jin-Hyun (2001) In Molecular Biotechnology 18(3). p.193-198
Abstract
A magainin derivative, designated MSI-344, was produced in Escherichia coli as fusion protein, by utilizing a truncated amidophsphoribosyltransferase of E. coli
as a fusion partner. Bacterial cells transformed with the gene encoding
the fusion protein were grown to a high cell density and induced with
isopropyl-1-thio-b-D-galatoside (IPTG) to initiate product expression.
The fusion protein was accumulated into cytoplasmic inclusion body and
recombinant MSI-344 was released from the fusion partner by
hydroxylamine treatment. Following cleavage of the fusion protein with
hydroxylamine, the released MSI-344 was purified to homogeneity by
cationic exchange chromatography. The final purity... (More)
A magainin derivative, designated MSI-344, was produced in Escherichia coli as fusion protein, by utilizing a truncated amidophsphoribosyltransferase of E. coli
as a fusion partner. Bacterial cells transformed with the gene encoding
the fusion protein were grown to a high cell density and induced with
isopropyl-1-thio-b-D-galatoside (IPTG) to initiate product expression.
The fusion protein was accumulated into cytoplasmic inclusion body and
recombinant MSI-344 was released from the fusion partner by
hydroxylamine treatment. Following cleavage of the fusion protein with
hydroxylamine, the released MSI-344 was purified to homogeneity by
cationic exchange chromatography. The final purity was at least 95% by
reversed-phase high performance liquid chromatography (RP-HPLC).
Purified recombinant MSI-344 was found to be indistinguishable from the
synthetic peptide determined by amino acid sequences and antimicrobial
activity assay. (Less)
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author
; ; ; ; ; ; and
publishing date
type
Contribution to journal
publication status
published
in
Molecular Biotechnology
volume
18
issue
3
pages
6 pages
publisher
Humana Press
external identifiers
  • scopus:0034943549
ISSN
1559-0305
DOI
10.1385/MB:18:3:193
language
English
LU publication?
no
id
d9afebb8-14a3-452b-85fd-08896dc00cec
date added to LUP
2025-09-05 17:48:01
date last changed
2025-09-17 12:27:49
@article{d9afebb8-14a3-452b-85fd-08896dc00cec,
  abstract     = {{A magainin derivative, designated MSI-344, was produced in <i>Escherichia coli</i> as fusion protein, by utilizing a truncated amidophsphoribosyltransferase of <i>E. coli</i><br>
 as a fusion partner. Bacterial cells transformed with the gene encoding<br>
 the fusion protein were grown to a high cell density and induced with <br>
isopropyl-1-thio-b-D-galatoside (IPTG) to initiate product expression. <br>
The fusion protein was accumulated into cytoplasmic inclusion body and <br>
recombinant MSI-344 was released from the fusion partner by <br>
hydroxylamine treatment. Following cleavage of the fusion protein with <br>
hydroxylamine, the released MSI-344 was purified to homogeneity by <br>
cationic exchange chromatography. The final purity was at least 95% by <br>
reversed-phase high performance liquid chromatography (RP-HPLC). <br>
Purified recombinant MSI-344 was found to be indistinguishable from the <br>
synthetic peptide determined by amino acid sequences and antimicrobial <br>
activity assay.}},
  author       = {{Hwang, Sung-Wook and Lee, Jae-Hyun and Park, Heung-Bok and Pyo, Sang-Hyun and So, Jin-Eon and Lee, Hyun-Soo and Hong, Seung-Suh and Kim, Jin-Hyun}},
  issn         = {{1559-0305}},
  language     = {{eng}},
  number       = {{3}},
  pages        = {{193--198}},
  publisher    = {{Humana Press}},
  series       = {{Molecular Biotechnology}},
  title        = {{A simple method for the purification of an antimicrobial peptide in recombinant <i>Escherichia coli</i>}},
  url          = {{http://dx.doi.org/10.1385/MB:18:3:193}},
  doi          = {{10.1385/MB:18:3:193}},
  volume       = {{18}},
  year         = {{2001}},
}