A DNA Spiegelmer to staphylococcal enterotoxin B

Details

Serval ID
serval:BIB_4D57CD7E71F1
Type
Article: article from journal or magazin.
Collection
Publications
Institution
Title
A DNA Spiegelmer to staphylococcal enterotoxin B
Journal
Nucleic Acids Research
Author(s)
Purschke  W. G., Radtke  F., Kleinjung  F., Klussmann  S.
ISSN
1362-4962 (Electronic)
Publication state
Published
Issued date
06/2003
Volume
31
Number
12
Pages
3027-32
Notes
Journal Article
Research Support, Non-U.S. Gov't --- Old month value: Jun 15
Abstract
Bacterial staphylococcal enterotoxin B is involved in several severe disease patterns and it was therefore used as a target for the generation of biologically stable mirror-image oligonucleotide ligands, so called Spiegelmers. The toxin is a 28 kDa protein consisting of 239 amino acids. Since the full-length protein is not accessible to chemical peptide synthesis, a stable domain of 25 amino acids was identified as a suitable selection target. DNA in vitro selection experiments were carried out against the equivalent mirror-image D-peptide domain resulting in high affinity D-DNA aptamers. As expected, the corresponding enantiomeric L-DNA Spiegelmer showed comparable binding characteristics to the L-peptide domain. Moreover, the Spiegelmer bound the whole protein target with only slightly reduced affinity. Dissociation constants of both peptide-oligonucleotide complexes were measured in the range of 200 nM, whereas the Spiegelmer binding to the full-length protein was determined at approximately 420 nM. These data demonstrate the possibility to identify Spiegelmers against large protein targets by a domain approach.
Keywords
Base Sequence DNA/chemistry/metabolism Enterotoxins/*chemistry/*metabolism Ligands Models, Molecular Molecular Sequence Data Nucleic Acid Conformation Oligodeoxyribonucleotides/chemistry/*metabolism Peptides/metabolism Protein Structure, Tertiary
Pubmed
Web of science
Open Access
Yes
Create date
28/01/2008 11:39
Last modification date
20/08/2019 14:02
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