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Selection of cadmium specific hexapeptides and their expression as OmpA fusion proteins in Escherichia coli

Mejàre, M LU ; Ljung, Sarah and Bülow, L LU (1998) In Protein Engineering 11(6). p.94-489
Abstract

In searching for novel peptides with affinity for cadmium, the phage display technique was utilized. In the selection procedure, cadmium ions were immobilized on a metal chelating Sepharose gel. The peptides selected from a hexapeptide library showed no homology to naturally occurring metallothioneins. From the phage clones selected in the biopanning process, phages with affinity for Cd-109 in free solution were identified. The peptide His-Ser-Gln-Lys-Val-Phe, which was found to exhibit the strongest relative affinity for Cd-109, was cloned into Escherichia coli as a fusion to the cell surface exposed area of the outer membrane protein OmpA. Escherichia coli cells expressing this peptide showed increased survival in growth media... (More)

In searching for novel peptides with affinity for cadmium, the phage display technique was utilized. In the selection procedure, cadmium ions were immobilized on a metal chelating Sepharose gel. The peptides selected from a hexapeptide library showed no homology to naturally occurring metallothioneins. From the phage clones selected in the biopanning process, phages with affinity for Cd-109 in free solution were identified. The peptide His-Ser-Gln-Lys-Val-Phe, which was found to exhibit the strongest relative affinity for Cd-109, was cloned into Escherichia coli as a fusion to the cell surface exposed area of the outer membrane protein OmpA. Escherichia coli cells expressing this peptide showed increased survival in growth media containing up to 1.2 mM CdCl2 when compared with cells not expressing this peptide on their surface.

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Contribution to journal
publication status
published
subject
keywords
Amino Acid Sequence, Bacterial Outer Membrane Proteins, Bacteriophages, Cadmium, Cadmium Chloride, Chelating Agents, Culture Media, Escherichia coli, Gene Expression, Gene Library, Oligopeptides, Plasmids, Recombinant Fusion Proteins, Sepharose, Structure-Activity Relationship, Zinc
in
Protein Engineering
volume
11
issue
6
pages
6 pages
publisher
Oxford University Press
external identifiers
  • scopus:0347064880
ISSN
0269-2139
DOI
10.1093/protein/11.6.489
language
English
LU publication?
yes
id
5e3dd87e-f761-4875-a36f-cf12b6e38a05
date added to LUP
2016-04-18 15:59:55
date last changed
2017-05-02 19:34:14
@article{5e3dd87e-f761-4875-a36f-cf12b6e38a05,
  abstract     = {<p>In searching for novel peptides with affinity for cadmium, the phage display technique was utilized. In the selection procedure, cadmium ions were immobilized on a metal chelating Sepharose gel. The peptides selected from a hexapeptide library showed no homology to naturally occurring metallothioneins. From the phage clones selected in the biopanning process, phages with affinity for Cd-109 in free solution were identified. The peptide His-Ser-Gln-Lys-Val-Phe, which was found to exhibit the strongest relative affinity for Cd-109, was cloned into Escherichia coli as a fusion to the cell surface exposed area of the outer membrane protein OmpA. Escherichia coli cells expressing this peptide showed increased survival in growth media containing up to 1.2 mM CdCl2 when compared with cells not expressing this peptide on their surface.</p>},
  author       = {Mejàre, M and Ljung, Sarah and Bülow, L},
  issn         = {0269-2139},
  keyword      = {Amino Acid Sequence,Bacterial Outer Membrane Proteins,Bacteriophages,Cadmium,Cadmium Chloride,Chelating Agents,Culture Media,Escherichia coli,Gene Expression,Gene Library,Oligopeptides,Plasmids,Recombinant Fusion Proteins,Sepharose,Structure-Activity Relationship,Zinc},
  language     = {eng},
  number       = {6},
  pages        = {94--489},
  publisher    = {Oxford University Press},
  series       = {Protein Engineering},
  title        = {Selection of cadmium specific hexapeptides and their expression as OmpA fusion proteins in Escherichia coli},
  url          = {http://dx.doi.org/10.1093/protein/11.6.489},
  volume       = {11},
  year         = {1998},
}