ArticleInternational journal of molecular sciences2015
Structure-Based Optimization of Inhibitors of the Aspartic Protease Endothiapepsin.
Article in International journal of molecular sciences, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 4 papers.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
4 citing papers in PubMed, 15 citations in OpenAlex.
- pH-Dependent Structural Dynamics of Cathepsin D-Family Aspartic Peptidase ofPathogens (Basel, Switzerland) · 2021Article
- AnJournal of biomolecular structure & dynamics · 2021Article
- Urea-aromatic interactions in biology.Biophysical reviews · 2020Review
- Protein-Templated Dynamic Combinatorial Chemistry: Brief Overview and Experimental Protocol.European journal of organic chemistry · 2019Review
Corrections and comments
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Authors and funding
5 authors at 2 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Aspartic proteases are a class of enzymes that play a causative role in numerous diseases such as malaria (plasmepsins), Alzheimer's disease (β-secretase), fungal infections (secreted aspartic proteases), and hypertension (renin). We have chosen endothiapepsin as a model enzyme of this class of enzymes, for the design, preparation and biochemical evaluation of a new series of inhibitors of endothiapepsin. Here, we have optimized a hit, identified by de novo structure-based drug design (SBDD) and DCC, by using structure-based design approaches focusing on the optimization of an amide-π interaction. Biochemical results are in agreement with SBDD. These results will provide useful insights for future structure-based optimization of inhibitors for the real drug targets as well as insights into molecular recognition.
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Registered trials
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