ArticleProtein science : a publication of the Protein Society1997
Structure-based subsite specificity mapping of human cathepsin D using statine-based inhibitors.
Article in Protein science : a publication of the Protein Society, 1997. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 4 papers.
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4 citing papers in PubMed, 43 citations in OpenAlex.
- Computational Workflow to Design Novel Vaccine Candidates and Small-Molecule Therapeutics for Schistosomiasis.Pathogens (Basel, Switzerland) · 2024Article
- A fluorogenic, peptide-based probe for the detection of Cathepsin D in macrophages.Communications chemistry · 2023Article
- New cathepsin D inhibitor library utilizing hydroxyethyl isosteres with cyclic tertiary amines.Medicinal chemistry (Shariqah (United Arab Emirates)) · 2012Article
- Hemoglobin digestion in blood-feeding ticks: mapping a multipeptidase pathway by functional proteomics.Chemistry & biology · 2009Article
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4 authors at 3 institutions in 1 country.
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Abstract
Human cathepsin D is a lysosomal aspartic protease that has been implicated in breast cancer metastasis and Alzheimer's disease. Based on a crystal structure of a human cathepsin D-pepstatin A complex, a series of statine-containing inhibitors was designed, synthesized, and tested for inhibitory activity toward the enzyme in vitro. The compounds were modified systematically at individual positions (P4, P3, P2, P1, and P2t) with the aim of mapping the cathepsin D subsite preferences. The experimentally obtained SAR data were correlated on the basis of molecular modeling. Side-chain preferences for the peptidomimetic inhibitors differed from those found previously using peptide substrates (Scarborough PE et al., 1993, Protein Sci 2:264-276). In addition, the effects of single side-chain modifications were often nonadditive. Structure-activity relationships, modeling, and thermodynamic analysis indicated that entropy plays a major stabilizing role in inhibitor binding to cathepsin D.
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