ArticleThe Journal of biological chemistry2010
Proline periodicity modulates the self-assembly properties of elastin-like polypeptides.
Article in The Journal of biological chemistry, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 25 papers.
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Who cites it
25 citing papers in PubMed.
- Evolutionary constraints on positional sequence, collective properties and sequence style of tropoelastin dictated by fundamental requirements for formation and function of the extracellular elastic matrix.Matrix biology plus · 2025Review
- Discovery of unconventional and nonintuitive self-assembling peptide materials using experiment-driven machine learning.Science advances · 2025Article
- Bridging Nature and Engineering: Protein-Derived Materials for Bio-Inspired Applications.Biomimetics (Basel, Switzerland) · 2024Review
- Synthetic intrinsically disordered protein fusion tags that enhance protein solubility.Nature communications · 2024Article
- Crosstalk between protein post-translational modifications and phase separation.Cell communication and signaling : CCS · 2024Review
- Contribution of the ELRs to the development of advancedFrontiers in bioengineering and biotechnology · 2024Review
- Comprehensive Regulation of Liquid-Liquid Phase Separation of Polypeptides.Molecules (Basel, Switzerland) · 2023Article
- Liquid to solid transition of elastin condensates.Proceedings of the National Academy of Sciences of the United States of America · 2022Article
- Using ELP Repeats as a Scaffold for De Novo Construction of Gadolinium-Binding Domains within Multifunctional Recombinant Proteins for Targeted Delivery of Gadolinium to Tumour Cells.International journal of molecular sciences · 2022Article
- Fast and reversible crosslinking of a silk elastin-like polymer.Acta biomaterialia · 2022Article
- Intrinsically disordered protein, DNA binding with one finger transcription factor (Frontiers in plant science · 2022Article
- De novo engineering of intracellular condensates using artificial disordered proteins.Nature chemistry · 2020Article
- Article
- Self-assembly in elastin-like recombinamers: a mechanism to mimic natural complexity.Materials today. Bio · 2019Review
- Squid-Inspired Tandem Repeat Proteins: Functional Fibers and Films.Frontiers in chemistry · 2019Review
- Genetically encoded lipid-polypeptide hybrid biomaterials that exhibit temperature-triggered hierarchical self-assembly.Nature chemistry · 2018Article
- Ubiquitin Modulates Liquid-Liquid Phase Separation of UBQLN2 via Disruption of Multivalent Interactions.Molecular cell · 2018Article
- Self-assembly/disassembly hysteresis of nanoparticles composed of marginally soluble, short elastin-like polypeptides.Journal of nanobiotechnology · 2018Article
- Refining Disordered Peptide Ensembles with Computational Amide I Spectroscopy: Application to Elastin-Like Peptides.The journal of physical chemistry. B · 2016Article
- Sequence heuristics to encode phase behaviour in intrinsically disordered protein polymers.Nature materials · 2015Article
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2 authors.
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Abstract
Elastin is a self-assembling protein of the extracellular matrix that provides tissues with elastic extensibility and recoil. The monomeric precursor, tropoelastin, is highly hydrophobic yet remains substantially disordered and flexible in solution, due in large part to a high combined threshold of proline and glycine residues within hydrophobic sequences. In fact, proline-poor elastin-like sequences are known to form amyloid-like fibrils, rich in β-structure, from solution. On this basis, it is clear that hydrophobic elastin sequences are in general optimized to avoid an amyloid fate. However, a small number of hydrophobic domains near the C terminus of tropoelastin are substantially depleted of proline residues. Here we investigated the specific contribution of proline number and spacing to the structure and self-assembly propensities of elastin-like polypeptides. Increasing the spacing between proline residues significantly decreased the ability of polypeptides to reversibly self-associate. Real-time imaging of the assembly process revealed the presence of smaller colloidal droplets that displayed enhanced propensity to cluster into dense networks. Structural characterization showed that these aggregates were enriched in β-structure but unable to bind thioflavin-T. These data strongly support a model where proline-poor regions of the elastin monomer provide a unique contribution to assembly and suggest a role for localized β-sheet in mediating self-assembly interactions.
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