ArticleBiopolymers2018
To achieve self-assembled collagen mimetic fibrils using designed peptides.
Article in Biopolymers, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.
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Who cites it
9 citing papers in PubMed.
- Designed Fibril-Forming Mini-Collagens Engineered to Exhibit up to Two Orders of Magnitude Differences in Rates of Matrix Metalloproteinase I Susceptibility.Biomacromolecules · 2025Article
- Diffusion model assisted designing self-assembling collagen mimetic peptides as biocompatible materials.Briefings in bioinformatics · 2024Article
- Using sequence data to predict the self-assembly of supramolecular collagen structures.Biophysical journal · 2022Article
- Segment-Long-Spacing (SLS) and the Polymorphic Structures of Fibrillar Collagen.Sub-cellular biochemistry · 2022Review
- Collagen Mimetic Peptides.Bioengineering (Basel, Switzerland) · 2021Review
- Engineered Collagen Matrices.Bioengineering (Basel, Switzerland) · 2020Review
- Photo-responsive azobenzene interactions promote hierarchical self-assembly of collagen triple-helical peptides to various higher-order structures.RSC advances · 2020Article
- The predominant roles of the sequence periodicity in the self-assembly of collagen-mimetic mini-fibrils.Protein science : a publication of the Protein Society · 2019Article
- Characterization by high-resolution crystal structure analysis of a triple-helix region of human collagen type III with potent cell adhesion activity.Biochemical and biophysical research communications · 2019Article
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Authors and funding
7 authors.
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Abstract
It has proven challenging to obtain collagen-mimetic fibrils by protein design. We recently reported the self-assembly of a mini-fibril showing a 35 nm, D-period like, axially repeating structure using the designed triple helix Col108. Peptide Col108 was made by bacterial expression using a synthetic gene; its triple helix domain consists of three pseudo-identical units of amino acid sequence arranged in tandem. It was postulated that the 35 nm d-period of Col108 mini-fibrils originates from the periodicity of the Col108 primary structure. A mutual staggering of one sequence unit of the associating Col108 triple helices can maximize the inter-helical interactions and produce the observed 35 nm d-period. Based on this unit-staggered model, a triple helix consisting of only two sequence units is expected to have the potential to form the same d-periodic mini-fibrils. Indeed, when such a peptide, peptide 2U108, was made it was found to self-assemble into mini-fibrils having the same d-period of 35 nm. In contrast, no d-periodic mini-fibrils were observed for peptide 1U108, which does not have long-range repeating sequences in its primary structure. The findings of the periodic mini-fibrils of Col108 and 2U108 suggest a way forward to create collagen-mimetic fibrils for biomedical and industrial applications.
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