ArticleChemical science2022
Terminal repeats impact collagen triple-helix stability through hydrogen bonding.
Article in Chemical science, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.
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Who cites it
17 citing papers in PubMed, 35 citations in OpenAlex.
- Exploration of tropocollagen unwinding by cathepsin K dimer with chondroitin 4-sulphate through microsecond timescale molecular dynamics.Journal of enzyme inhibition and medicinal chemistry · 2026Article
- Extraction, characterization and antioxidant activity evaluation of collagen from Monopterus albus bones.Journal of the science of food and agriculture · 2026Article
- Bioprinting in Tissue Repair and Its ENT Applications.Polymers · 2026Review
- Formation of S- and Z-twist supramolecular micro-ropes by peptide stereoisomers.Nature communications · 2026Article
- Article
- Modulating Refolding and Collagen Binding of Collagen Hybridizing Peptides through Peptoid Incorporation.Biomacromolecules · 2026Article
- Preparation and Characterization of Eel (Foods (Basel, Switzerland) · 2025Article
- Thermally Cured Gelatin-Methacryloyl Hydrogels Form Mechanically Modulating Platforms for Cell Studies.Biomacromolecules · 2025Article
- β-Turn Mimicking Crosslinking Provides Hyperstability and Fast Folding Kinetics for Short Collagen Triple Helices.Chembiochem : a European journal of chemical biology · 2025Article
- Exploration of the hierarchical assembly space of collagen-like peptides beyond the triple helix.Nature communications · 2024Article
- Promoting chondrogenesis by targeted delivery to the degenerating cartilage in early treatment of osteoarthritis.Bioactive materials · 2024Article
- Textural, rheological, and structural properties of turkey and chicken gelatins from mechanical deboning residues.Food science & nutrition · 2024Article
- Beyond the Triple Helix: Exploration of the Hierarchical Assembly Space of Collagen-like Peptides.bioRxiv : the preprint server for biology · 2024Article
- From medical strategy to foodborne prophylactic strategy: Stabilizing dental collagen with aloin.Food science & nutrition · 2024Article
- Cis-trans isomerization of peptoid residues in the collagen triple-helix.Nature communications · 2023Article
- Hollow Octadecameric Self-Assembly of Collagen-like Peptides.Journal of the American Chemical Society · 2023Article
- Predicting Collagen Triple Helix Stability through Additive Effects of Terminal Residues and Caps.Angewandte Chemie (International ed. in English) · 2023Article
Corrections and comments
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Authors and funding
8 authors at 3 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Nearly 30% of human proteins have tandem repeating sequences. Structural understanding of the terminal repeats is well-established for many repeat proteins with the common α-helix and β-sheet foldings. By contrast, the sequence-structure interplay of the terminal repeats of the collagen triple-helix remains to be fully explored. As the most abundant human repeat protein and the most prevalent structural component of the extracellular matrix, collagen features a hallmark triple-helix formed by three supercoiled polypeptide chains of long repeating sequences of the Gly-X-Y triplets. Here, with CD characterization of 28 collagen-mimetic peptides (CMPs) featuring various terminal motifs, as well as DSC measurements, crystal structure analysis, and computational simulations, we show that CMPs only differing in terminal repeat may have distinct end structures and stabilities. We reveal that the cross-chain hydrogen bonding mediated by the terminal repeat is key to maintaining the triple-helix's end structure, and that disruption of it with a single amide to carboxylate substitution can lead to destabilization as drastic as 19 °C. We further demonstrate that the terminal repeat also impacts how strong the CMP strands form hybrid triple-helices with unfolded natural collagen chains in tissue. Our findings provide a spatial profile of hydrogen bonding within the CMP triple-helix, marking a critical guideline for future crystallographic or NMR studies of collagen, and algorithms for predicting triple-helix stability, as well as peptide-based collagen assemblies and materials. This study will also inspire new understanding of the sequence-structure relationship of many other complex structural proteins with repeating sequences.
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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.