ArticleThe Journal of biological chemistry2014
Conformational transitions of the cross-linking domains of elastin during self-assembly.
Article in The Journal of biological chemistry, 2014. 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, 58 citations in OpenAlex.
- Construction and expression of recombinant human elastin with biological activities: effect of wound healingFrontiers in bioengineering and biotechnology · 2026Article
- 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
- Beyond the Critical Threshold: Elastic Fiber Remodeling and Fracture in the Pathogenesis of Pulmonary Emphysema.International journal of molecular sciences · 2025Review
- Article
- Contribution of the ELRs to the development of advancedFrontiers in bioengineering and biotechnology · 2024Review
- Physicochemical Characterization of a Biomimetic, Elastin-Inspired Polypeptide with Enhanced Thermoresponsive Properties and Improved Cell Adhesion.Biomacromolecules · 2023Article
- Construction of a Collagen-like Protein Based on Elastin-like Polypeptide Fusion and Evaluation of Its Performance in Promoting Wound Healing.Molecules (Basel, Switzerland) · 2023Article
- Elastin-Hyaluronan Bioconjugate as Bioactive Component in Electrospun Scaffolds.Chemistry (Weinheim an der Bergstrasse, Germany) · 2022Article
- Fuzzy binding model of molecular interactions between tropoelastin and integrin alphaVbeta3.Biophysical journal · 2021Article
- Folding and self-assembly of short intrinsically disordered peptides and protein regions.Nanoscale advances · 2021Review
- Tropoelastin and Elastin Assembly.Frontiers in bioengineering and biotechnology · 2021Review
- Lysyl oxidase-like 2 (LOXL2)-mediated cross-linking of tropoelastin.FASEB journal : official publication of the Federation of American Societies for Experimental Biology · 2019Article
- Fusion of fibroblast growth factor 21 to a thermally responsive biopolymer forms an injectable depot with sustained anti-diabetic action.Journal of controlled release : official journal of the Controlled Release Society · 2018Article
- Direct observation of structure and dynamics during phase separation of an elastomeric protein.Proceedings of the National Academy of Sciences of the United States of America · 2017Article
- The Coupled Bio-Chemo-Electro-Mechanical Behavior of Glucose Exposed Arterial Elastin.Journal of physics D: Applied physics · 2017Article
- Quarterly intrinsic disorder digest (April-May-June, 2014).Intrinsically disordered proteins · 2017Article
- Elastin-like polypeptides: Therapeutic applications for an emerging class of nanomedicines.Journal of controlled release : official journal of the Controlled Release Society · 2016Review
Corrections and comments
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Authors and funding
6 authors at 2 institutions in 1 country.
Funding
Abstract
Elastin is the intrinsically disordered polymeric protein imparting the exceptional properties of extension and elastic recoil to the extracellular matrix of most vertebrates. The monomeric precursor of elastin, tropoelastin, as well as polypeptides containing smaller subsets of the tropoelastin sequence, can self-assemble through a colloidal phase separation process called coacervation. Present understanding suggests that self-assembly is promoted by association of hydrophobic domains contained within the tropoelastin sequence, whereas polymerization is achieved by covalent joining of lysine side chains within distinct alanine-rich, α-helical cross-linking domains. In this study, model elastin polypeptides were used to determine the structure of cross-linking domains during the assembly process and the effect of sequence alterations in these domains on assembly and structure. CD temperature melts indicated that partial α-helical structure in cross-linking domains at lower temperatures was absent at physiological temperature. Solid-state NMR demonstrated that β-strand structure of the cross-linking domains dominated in the coacervate state, although α-helix was predominant after subsequent cross-linking of lysine side chains with genipin. Mutation of lysine residues to hydrophobic amino acids, tyrosine or alanine, leads to increased propensity for β-structure and the formation of amyloid-like fibrils, characterized by thioflavin-T binding and transmission electron microscopy. These findings indicate that cross-linking domains are structurally labile during assembly, adapting to changes in their environment and aggregated state. Furthermore, the sequence of cross-linking domains has a dramatic effect on self-assembly properties of elastin-like polypeptides, and the presence of lysine residues in these domains may serve to prevent inappropriate ordered aggregation.
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