Designing a polyvalent inhibitor of anthrax toxin View Full Text


Ontology type: schema:ScholarlyArticle     


Article Info

DATE

2001-10

AUTHORS

M Mourez, R S Kane, J Mogridge, S Metallo, P Deschatelets, B R Sellman, G M Whitesides, R J Collier

ABSTRACT

Screening peptide libraries is a proven strategy for identifying inhibitors of protein-ligand interactions. Compounds identified in these screens often bind to their targets with low affinities. When the target protein is present at a high density on the surface of cells or other biological surfaces, it is sometimes possible to increase the biological activity of a weakly binding ligand by presenting multiple copies of it on the same molecule. We isolated a peptide from a phage display library that binds weakly to the heptameric cell-binding subunit of anthrax toxin and prevents the interaction between cell-binding and enzymatic moieties. A molecule consisting of multiple copies of this nonnatural peptide, covalently linked to a flexible backbone, prevented assembly of the toxin complex in vitro and blocked toxin action in an animal model. This result demonstrates that protein-protein interactions can be inhibited by a synthetic, polymeric, polyvalent inhibitor in vivo. More... »

PAGES

958-961

Journal

TITLE

Nature Biotechnology

ISSUE

10

VOLUME

19

Author Affiliations

Identifiers

URI

http://scigraph.springernature.com/pub.10.1038/nbt1001-958

DOI

http://dx.doi.org/10.1038/nbt1001-958

DIMENSIONS

https://app.dimensions.ai/details/publication/pub.1031033371

PUBMED

https://www.ncbi.nlm.nih.gov/pubmed/11581662


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