ArticleProtein science : a publication of the Protein Society2009
Proligands with protease-regulated binding activity identified from cell-displayed prodomain libraries.
Article in Protein science : a publication of the Protein Society, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.
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Who cites it
7 citing papers in PubMed.
- Exploiting protease activation for therapy.Drug discovery today · 2022Review
- Switchable immune modulator for tumor-specific activation of anticancer immunity.Science advances · 2021Article
- FimH as a scaffold for regulated molecular recognition.Journal of biological engineering · 2021Article
- A coiled-coil masking domain for selective activation of therapeutic antibodies.Nature biotechnology · 2019Article
- Selective antibody activation through protease-activated pro-antibodies that mask binding sites with inhibitory domains.Scientific reports · 2017Article
- Getting physical to fix pharma.Nature chemistry · 2011Article
- Screening of peptide libraries against protective antigen of Bacillus anthracis in a disposable microfluidic cartridge.PloS one · 2011Article
Corrections and comments
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Authors and funding
2 authors.
Funding
Abstract
A general method was developed for the discovery of protease-activated binding ligands, or proligands, from combinatorial prodomain libraries displayed on the surface of E. coli. Peptide libraries of candidate prodomains were fused with a matrix metalloprotease-2 substrate linker to a vascular endothelial growth factor-binding peptide and sorted using a two-stage flow cytometry screening procedure to isolate proligands that required protease treatment for binding activity. Prodomains that imparted protease-mediated switching activity were identified after three sorting cycles using two unique library design strategies. The best performing proligand exhibited a 100-fold improvement in apparent binding affinity after exposure to protease. This method may prove useful for developing therapeutic and diagnostic ligands with improved systemic targeting specificity.
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