ArticleBiomacromolecules2026
Structural and Positional Effects of Peptoid Residues on Triple Helix Stability.
Article in Biomacromolecules, 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 2 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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Who cites it
2 citing papers in PubMed.
- Modulating Refolding and Collagen Binding of Collagen Hybridizing Peptides through Peptoid Incorporation.Biomacromolecules · 2026Article
- From Collagen Mimetics to Collagen Hybridization and Back.Accounts of chemical research · 2024Article
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Authors and funding
10 authors.
Funding
Abstract
The collagen triple helix, composed of three protein strands with a repeating GlyXaaYaa sequence, achieves maximum stability with proline (Pro) and hydroxyproline (Hyp) at the Xaa and Yaa positions. Previously, we demonstrated that peptoid residues (N-substituted glycines, N-Glys) at the Xaa position significantly enhance the triple helix stability. Here, we show that N-Glys at the Yaa position also stabilize the triple helix, with stability influenced by the N-Gly's position and side chain structure. Over 22 N-Glys with various natural and unnatural side chains were investigated using CD spectroscopy, X-ray crystallography, and computational simulations. The results show that N-Glys at the Yaa position support triple helical folding and are more stabilizing than their corresponding amino acids but less so than Hyp due to suboptimal ϕ-ψ angles. Metadynamics simulations revealed that N-Glys at the Yaa position have a broader conformational space due to minimal steric hindrance from neighboring glycine residues. N-Glys' side chain bulkiness influenced stability only at the Xaa position and not the Yaa position. Additionally, only
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Registered trials
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