The design, synthesis and evaluation of affinity ligands for prion proteins

Bifunctional affinity ligands based on a triazine scaffold were rationally designed to target prion protein and shown to bind recombinant prion protein with high affinity and selectivity. The ligands were capable of discriminating between prion protein glycoforms and monomeric and dimeric forms of t...

Full description

Saved in:
Bibliographic Details
Published in:Journal of molecular recognition 2004-05, Vol.17 (3), p.248-261
Main Authors: Renou, Emma N. Soto, Gupta, Geeta, Young, Duncan S., Dear, Denise V., Lowe, Christopher R.
Format: Article
Language:English
Subjects:
affinity ligands
Animals
Binding Sites
Drug Evaluation, Preclinical
Ligands
Models, Molecular
Mutation - genetics
prion protein
Prions - chemistry
Prions - genetics
Prions - metabolism
Protein Binding
Protein Structure, Quaternary
rational design
Sheep
solid phase combinatorial chemistry
triazine
Triazines - chemical synthesis
Triazines - chemistry
Triazines - metabolism
Citations: Items that this one cites
Items that cite this one
Online Access:Get full text
Tags: Add Tag
No Tags, Be the first to tag this record!
Description
Summary:Bifunctional affinity ligands based on a triazine scaffold were rationally designed to target prion protein and shown to bind recombinant prion protein with high affinity and selectivity. The ligands were capable of discriminating between prion protein glycoforms and monomeric and dimeric forms of the prion protein. The ligands also discriminate between conformational differences in the prion protein, resulting from point mutations in the prion protein gene. These results suggest that derived compounds could be used selectively to detect the disease‐associated form of the prion protein, and as such, could provide diagnostic or therapeutic tools for prion diseases. Copyright © 2004 John Wiley & Sons, Ltd.
ISSN:0952-3499
1099-1352
DOI:10.1002/jmr.670