ArticleRSC chemical biology2020
Long-range PEG Stapling: Macrocyclization for Increased Protein Conformational Stability and Resistance to Proteolysis.
Article in RSC chemical biology, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers.
What it found
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The trial behind it
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Who cites it
6 citing papers in PubMed.
- Folded-state compatibility and unfolded-state constraint govern staple-based stabilization: guidelines from a coiled-coil model.RSC chemical biology · 2026Article
- The Minimum Protein Staple? - Towards 'bio'-Baldwin's rulesChemical science · 2024Article
- Genetically encoded discovery of perfluoroaryl macrocycles that bind to albumin and exhibit extended circulation in vivo.Nature communications · 2023Article
- Structural guidelines for stabilization of α-helical coiled coilsRSC chemical biology · 2022Article
- Protein Macrocyclization for Tertiary Structure Stabilization.Chembiochem : a European journal of chemical biology · 2021Review
- Accessing Improbable Foldamer Shapes with Strained Macrocycles.Chemistry (Weinheim an der Bergstrasse, Germany) · 2021Article
Corrections and comments
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Authors and funding
5 authors.
Funding
Abstract
We previously showed that long-range stapling of two Asn-linked O-allyl PEG oligomers via olefin metathesis substantially increases the conformational stability of the WW domain through an entropic effect. The impact of stapling was more favorable when the staple connected positions that were far apart in primary sequence but close in the folded tertiary structure. Here we validate these criteria for identifying new stabilizing PEG-stapling sites within the WW domain and the SH3 domain, both β-sheet proteins. We find that stapling via olefin metathesis vs. the copper(I)-catalyzed azide/alkyne cycloaddition (CuAAC) results in similar energetic benefits, suggesting that olefin and triazole staples can be used interchangeably. Proteolysis assays of selected WW variants reveal that the observed staple-based increases in conformational stability lead to enhanced proteolytic resistance. Finally, we find that an intermolecular staple dramatically increases the quaternary structural stability of an α-helical GCN4 coiled-coil heterodimer.
Identifiers
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Registered trials
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