ArticleAngewandte Chemie (International ed. in English)2021
Sequence-Selective Protection of Peptides from Proteolysis.
Article in Angewandte Chemie (International ed. in English), 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.
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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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Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
8 citing papers in PubMed.
- Substrate-Selective Inhibition of the SARS-CoV-2 Papain-Like Protease: Inhibition of Hydrolysis of Human Over Viral Substrates.Chemistry (Weinheim an der Bergstrasse, Germany) · 2026Article
- Inhibition of protein-protein interactions among tubulinsRSC advances · 2026Article
- Amyloid-reoriented enzyme catalysis.Nature communications · 2025Article
- Molecularly imprinted materials for glycan recognition and processing.Journal of materials chemistry. B · 2022Review
- Review
- Epitope-imprinted polymers: Design principles of synthetic binding partners for natural biomacromolecules.Science advances · 2021Article
- Substrate Protection in Controlled Enzymatic Transformation of Peptides and Proteins.Chembiochem : a European journal of chemical biology · 2021Article
- Sequence-Selective Protection of Peptides from Proteolysis.Angewandte Chemie (International ed. in English) · 2021Article
Corrections and comments
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Authors and funding
3 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Proteolysis of proteins and peptides is involved in the infection of cells by enveloped viruses and also in the invasion and spread of cancer cells. Shutting down broad-specificity proteases, however, is problematic because normal functions by these proteases will be affected. Herein, nanoparticle receptors were prepared from molecular imprinting for complex biological peptides. Their strong and selective binding enabled them to protect their targeted sequences from proteolysis in aqueous solution at stoichiometric amounts. Generality of the method was demonstrated by the protection of hydrophobic and hydrophilic peptides from different proteases, selective protection of a segment of a long peptide, and selective protection of a targeted peptide in a mixture. Most interestingly, two receptors targeting different parts of a long peptide could work in cooperation to protect the overall sequence, highlighting the versatility of the method.
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Registered trials
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