ArticleThe Journal of biological chemistry2019
Disulfide engineering of human Kunitz-type serine protease inhibitors enhances proteolytic stability and target affinity toward mesotrypsin.
Article in The Journal of biological chemistry, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.
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Who cites it
15 citing papers in PubMed.
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- Formation of the intradimer disulfide bond in human calprotectin maintains metal-withholding function and tunes proteolytic susceptibility.Chemical science · 2026Article
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- F4, a collagen XIX-derived peptide, inhibits tumor angiogenesis through αvβ3 and α5β1 integrin interaction.Cell adhesion & migration · 2021Article
- Potent Inhibitor of Human Trypsins from the Aeruginosin Family of Natural Products.ACS chemical biology · 2021Article
- Trypsin-Like Proteases and Their Role in Muco-Obstructive Lung Diseases.International journal of molecular sciences · 2021Review
- Protease-stable DARPins as promising oral therapeutics.Protein engineering, design & selection : PEDS · 2021Article
- Evolutionary Aspects of the Structural Convergence and Functional Diversification of Kunitz-Domain Inhibitors.Journal of molecular evolution · 2020Review
- Miniproteins as a Powerful Modality in Drug Development.Trends in biochemical sciences · 2020Review
- Cysteines and Disulfide Bonds as Structure-Forming Units: Insights From Different Domains of Life and the Potential for Characterization by NMR.Frontiers in chemistry · 2020Review
- Genomic Observations of a Rare/PathogenicMedicina (Kaunas, Lithuania) · 2019Article
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Authors and funding
9 authors.
Funding
Abstract
Serine protease inhibitors of the Kunitz-bovine pancreatic trypsin inhibitor (BPTI) family are ubiquitous biological regulators of proteolysis. These small proteins are resistant to proteolysis, but can be slowly cleaved within the protease-binding loop by target proteases, thereby compromising their activity. For the human protease mesotrypsin, this cleavage is especially rapid. Here, we aimed to stabilize the Kunitz domain structure against proteolysis through disulfide engineering. Substitution within the Kunitz inhibitor domain of the amyloid precursor protein (APPI) that incorporated a new disulfide bond between residues 17 and 34 reduced proteolysis by mesotrypsin 74-fold. Similar disulfide engineering of tissue factor pathway inhibitor-1 Kunitz domain 1 (
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