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- W1989464052 abstract "Elastin is the self-assembling extracellular matrix protein that provides elasticity to tissues. A fundamental requirement for forming elastomeric materials is retention of a high degree of conformational disorder even when aggregated. Elastin disorder is strongly related to a high (50%) combined proportion of proline and glycine residues within hydrophobic domains. The majority of elastin hydrophobic domains have an average proline spacing of 4-8 residues. However, the native sequence of hydrophobic domain 30 (D30) is uncharacteristically proline-poor. Here we investigated the contribution of D30 and variants to the self-assembly and material properties of elastin-mimetic biomaterials. Addition of native D30 substantially stabilized the surface of assembled aggregates compared to proline-rich controls, suggesting the potential for interfacial order in mediating droplet growth, rigidity and interactions. Materials were stiffer, consistent with a greater number of contacts between monomers, were less resilient, and displayed less internal resistance to force. Conversely, mechanical properties were restored upon addition of the longer and glycine-rich rat D30, suggesting an important contribution to conformational entropy from domain length and high glycine content. Taken together, we hypothesize structured motifs and cross-linking density play key roles in modulating elastin assembly and mechanics." @default.
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- W1989464052 date "2013-01-01" @default.
- W1989464052 modified "2023-09-29" @default.
- W1989464052 title "Sequence and Structural Modulators of Elastin Assembly and Mechanical Properties" @default.
- W1989464052 doi "https://doi.org/10.1016/j.bpj.2012.11.312" @default.
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