A DNA Spiegelmer to staphylococcal enterotoxin B
Détails
ID Serval
serval:BIB_4D57CD7E71F1
Type
Article: article d'un périodique ou d'un magazine.
Collection
Publications
Institution
Titre
A DNA Spiegelmer to staphylococcal enterotoxin B
Périodique
Nucleic Acids Research
ISSN
1362-4962 (Electronic)
Statut éditorial
Publié
Date de publication
06/2003
Volume
31
Numéro
12
Pages
3027-32
Notes
Journal Article
Research Support, Non-U.S. Gov't --- Old month value: Jun 15
Research Support, Non-U.S. Gov't --- Old month value: Jun 15
Résumé
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.
Mots-clé
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
Oui
Création de la notice
28/01/2008 12:39
Dernière modification de la notice
20/08/2019 15:02