Novel Zn2+-chelating peptides selected from a fimbria-displayed random peptide library

Kjaergaard, K., Schembri, M. A. and Klemm, P. (2001) Novel Zn2+-chelating peptides selected from a fimbria-displayed random peptide library. Applied And Environmental Microbiology, 67 12: 5467-5473. doi:10.1128/AEM.67.12.5467-5473.2001

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Author Kjaergaard, K.
Schembri, M. A.
Klemm, P.
Title Novel Zn2+-chelating peptides selected from a fimbria-displayed random peptide library
Journal name Applied And Environmental Microbiology   Check publisher's open access policy
ISSN 0099-2240
Publication date 2001
Sub-type Article (original research)
DOI 10.1128/AEM.67.12.5467-5473.2001
Open Access Status File (Publisher version)
Volume 67
Issue 12
Start page 5467
End page 5473
Total pages 7
Place of publication Washington
Publisher Amer Soc Microbiology
Language eng
Abstract The display of peptide sequences on the surface of bacteria is a technology that offers exciting applications in biotechnology and medical research. Type 1 fimbriae are surface organelles of Escherichia coli which mediate D-mannose-sensitive binding to different host surfaces by virtue of the FimH adhesin. FimH is a component of the fimbrial organelle that can accommodate and display a diverse range of peptide sequences on the E. coli cell surface. In this study we have constructed a random peptide library in FimH. The library, consisting of similar to 40 million individual clones, was screened for peptide sequences that conferred on recombinant cells the ability to bind Zn2+. By serial selection, sequences that exhibited various degrees of binding affinity and specificity toward Zn2+ were enriched. None of the isolated sequences showed similarity to known Zn2+-binding proteins, indicating that completely novel Zn2+-binding peptide sequences had been isolated. By changing the protein scaffold system, we demonstrated that the Zn2+-binding seems to be uniquely mediated by the peptide insert and to be independent of the sequence of the carrier protein. These findings might be applied in the design of biomatrices for bioremediation purposes or in the development of sensors for detection of heavy metals.
Keyword Biotechnology & Applied Microbiology
Cholera-toxin Epitope
Type-1 Fimbriae
Combinatorial Libraries
Surface Display
Fimh Adhesin
Q-Index Code C1
Q-Index Status Provisional Code
Institutional Status Unknown

Document type: Journal Article
Sub-type: Article (original research)
Collection: School of Chemistry and Molecular Biosciences
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Citation counts: TR Web of Science Citation Count  Cited 30 times in Thomson Reuters Web of Science Article | Citations
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Created: Wed, 19 Sep 2007, 16:03:23 EST