ArticleRSC chemical biology2026
Backbone N-heteroatom substitution as a strategy to enhance peptide proteolytic stability.
Article in RSC chemical biology, 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.
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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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Authors and funding
3 authors.
Funding
Abstract
Peptide-based ligands are well-suited to engage large biomolecular surfaces but are often limited by rapid proteolytic degradation in biological environments. Backbone modification offers a direct means to disrupt protease recognition while preserving side chain functionality; however, many established approaches impose conformational constraints that compromise biological activity. Here, we evaluate backbone
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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.