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• W2009968270 abstract "Tropoelastin, the native monomeric form of elastin, and elastin-like polypeptides undergo a process of temperature-induced phase separation (coacervation) resulting in self-organization of a polymeric network that can subsequently be cross-linked into an elastomeric polymer. In this study, the rheological properties of a recombinantly produced polypeptide mimicking the sequences and domain arrangements of tropoelastin were investigated to understand post-coacervation changes in structure and assembly. This polypeptide, designated EP20-24-24, consisted of three hydrophobic domains of native human tropoelastin flanking two cross-linking domains. Temperature-induced formation of coacervate droplets resulted in a small increase in viscosity. A higher temperature produced a second temperature-dependent transition (Tv) to a gel state characterized by a much higher viscosity, strong shear thinning, and a high ratio of storage to loss moduli. This gel state was fully reversible if the temperature was immediately lowered. However, incubation above Tv for 60 min resulted in a further transformation of the network, limiting thermal reversibility of the gelation process. These results demonstrate that for elastin-like polypeptides mimicking the sequence and domain arrangements of tropoelastin, temperature-induced coacervation and transition of the coacervate to a gel-like state are distinguishable events with separate transition temperatures. Moreover, gels formed by these elastin-like polypeptides undergo a process of maturation, reducing the reversibility of the gel state." @default.
• W2009968270 created "2016-06-24" @default.
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• W2009968270 creator A5024836837 @default.
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• W2009968270 date "2009-09-01" @default.
• W2009968270 modified "2023-10-16" @default.
• W2009968270 title "Viscoelastic properties and gelation of an elastin-like polypeptide" @default.
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• W2009968270 doi "https://doi.org/10.1122/1.3177005" @default.
• W2009968270 hasPublicationYear "2009" @default.
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