ArticleAngewandte Chemie (International ed. in English)2022
Cystine Knot Peptides with Tuneable Activity and Mechanism.
Article in Angewandte Chemie (International ed. in English), 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.
What it found
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Who cites it
9 citing papers in PubMed, 12 citations in OpenAlex.
- Tangled Tail of Mechanically Interlocked Peptides.Journal of the American Chemical Society · 2026Review
- Tropical psychotria plants are a rich source for peptide inhibitors of human prolyl oligopeptidase.Natural products and bioprospecting · 2026Article
- Anticoagulation during Extracorporeal Membrane Oxygenation (ECMO): A Selective Inhibitor of Activated Factor XII Compared to Heparin in anACS pharmacology & translational science · 2025Article
- Redox signaling-mediated tumor extracellular matrix remodeling: pleiotropic regulatory mechanisms.Cellular oncology (Dordrecht, Netherlands) · 2024Review
- Stabilizing Scaffold for Short Peptides Based on Knottins.Current cancer drug targets · 2024Article
- Disulfide-constrained peptide scaffolds enable a robust peptide-therapeutic discovery platform.PloS one · 2024Article
- Discovery and Characterization of MaK: A Novel Knottin Antimicrobial Peptide fromInternational journal of molecular sciences · 2023Article
- Cystine Knot Peptides with Tuneable Activity and Mechanism.Angewandte Chemie (International ed. in English) · 2022Article
- Inhibition ofFrontiers in cellular and infection microbiology · 2022Article
Corrections and comments
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Authors and funding
9 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Knottins are topologically complex peptides that are stabilised by a cystine knot and have exceptionally diverse functions, including protease inhibition. However, approaches for tuning their activity in situ are limited. Here, we demonstrate separate approaches for tuning the activity of knottin protease inhibitors using light or streptavidin. We show that the inhibitory activity and selectivity of an engineered knottin can be controlled with light by activating a second mode of action that switches the inhibitor ON against new targets. Guided by a knottin library screen, we also identify a position in the inhibitor's binding loop that permits insertion of a biotin tag without impairing activity. Using streptavidin, biotinylated knottins with nanomolar affinity can be switched OFF in activity assays, and the anticoagulant activity of a factor XIIa inhibitor can be rapidly switched OFF in human plasma. Our findings expand the scope of engineered knottins for precisely controlling protein function.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.