ReviewThe Biochemical journal2026
Molecular foundations of collagen triple helical assembly: the central role of prolyl-4-hydroxylation.
Review in The Biochemical journal, 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.
- Marine-Derived Proteins: Individual Variability in Health Effects Across Protein Structure, Host Genetics, and Gut Microbiota.Comprehensive reviews in food science and food safety · 2026Review
- Collagen-Based Microspheres for Biomedical Applications in Drug Delivery and Tissue Engineering.Biomimetics (Basel, Switzerland) · 2026Review
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Authors and funding
3 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Collagen, the principal structural protein of the extracellular matrix, has been pivotal in the evolution of multicellular life. Among its posttranslational modifications (PTMs), prolyl-4-hydroxylation stands out as the most conserved and functionally critical. This hydroxylation not only facilitates polyproline II-like helicity in single collagen strands but also underpins the stability and integrity of the triple helix. In this review, we summarize the molecular foundations of collagen assembly, emphasizing both thermodynamic and stereo-electronic contributions of 4-hydroxyproline (4-Hyp). Insights from collagen-mimetic peptides are highlighted to elucidate main-chain torsional preferences, the positional dependence of proline ring puckering, and the correlation between 4-Hyp and enhanced thermal stability. Parallel discussions explore stereo-electronic effects revealed through quantum chemical studies, particularly charge-transfer interactions that modulate pyrrolidine ring conformation and peptide bond geometry. Finally, we summarize advances from periodic quantum mechanical calculations that quantify interstrand binding energies across different tripeptide motifs. Together, these findings provide a molecular-level perspective on how prolyl-4-hydroxylation has shaped the unique stability and evolution of collagenous helicity.
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Registered trials
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