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Showing 1–10 of 10 results
Advanced filters: Author: Jeffrey D. Hartgerink Clear advanced filters

  • The computational prediction of complex protein architectures has been used to design globular proteins, but the folding of collagen triple helices is difficult to predict. Here, a sequence-based scoring function for triple helix is developed and used to select sequences likely to self-assemble with high stability.

    • Jorge A. Fallas
    • Jeffrey D. Hartgerink
    Research
    Nature Communications
    Volume: 3, P: 1-8

  • Despite advances in machine learning approaches, de novo design of collagen-based materials remains difficult. In this study, based on the natural structure of the defense collagen family of proteins, designed triple helical peptide assemblies are found to form ribbons and a variety of bundled, porous architectures.

    • Le Tracy Yu
    • Mark A. B. Kreutzberger
    • Jeffrey D. Hartgerink
    ResearchOpen Access
    Nature Communications
    Volume: 15, P: 1-11

  • The mechanism of collagen heterotrimer folding is difficult to recapitulate synthetically. Now an ABC collagen mimetic heterotrimer has been designed that employs pairwise amino acid interactions, validated by X-ray crystallography, to promote composition- and register-specific assembly. The high specificity of its assembly leads to an increased rate of folding compared with similar collagen heterotrimers.

    • Carson C. Cole
    • Douglas R. Walker
    • Jeffrey D. Hartgerink
    Research
    Nature Chemistry
    Volume: 16, P: 1698-1704

  • Designed heterotrimers of collagen I, locked in three possible chain registers, enable structural and functional characterization of each permutation, leading to identification of the AAB heterotrimer as the most active and therefore likely to occur biologically.

    • Abhishek A. Jalan
    • Douglas Sammon
    • Richard W. Farndale
    Research
    Nature Chemical Biology
    Volume: 16, P: 423-429

  • Collagen-like peptides can self-assemble into hundreds of closely related triple helices. Now, an algorithm has been developed that predicts the most stable helix and the extent to which it will assemble to the exclusion of the competing helices. This information can help improve the understanding of triple helix design and assembly.

    • Douglas R. Walker
    • Sarah A. H. Hulgan
    • Jeffrey D. Hartgerink
    Research
    Nature Chemistry
    Volume: 13, P: 260-269

  • A short, synthetic peptide has been prepared that mimics much of the assembly process of natural collagen. Electrostatic interactions are used to create a sticky-ended structure, which in turn self-assembles through several levels of structural hierarchy from peptide to triple helix to nanofibre and finally to hydrogel.

    • Lesley E. R. O'Leary
    • Jorge A. Fallas
    • Jeffrey D. Hartgerink
    Research
    Nature Chemistry
    Volume: 3, P: 821-828

  • Peptides can self-assemble into gels that are able to control bleeding from surgical wounds within seconds of being applied. This new nano-haemostat could dramatically change the way surgery is performed in the future.

    • Jeffrey D. Hartgerink
    News & Views
    Nature Nanotechnology
    Volume: 1, P: 166-167