Artificial Protein Block Polymer Libraries Bearing Two SADs: Effects of Elastin Domain Repeats

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• 作者：Min Dai ; Jennifer Haghpanah ; Navjot Singh ; Eric W. Roth ; Alice Liang ; Raymond S. Tu ; Jin Kim Montclare
• 刊名：Biomacromolecules
• 出版年：2011
• 出版时间：December 12, 2011
• 年：2011
• 卷：12
• 期：12
• 页码：4240-4246
• 全文大小：357K
• 年卷期：v.12,no.12(December 12, 2011)
• ISSN：1526-4602

文摘

We have generated protein block polymer E<sub>nsub>C and CE<sub>nsub> libraries composed of two different self-assembling domains (SADs) derived from elastin (E) and the cartilage oligomeric matrix protein coiled-coil (C). As the E domain is shortened, the polymers exhibit an increase in inverse transition temperature (T<sub>tsub>); however, the range of temperature change differs dramatically between the E<sub>nsub>C and CE<sub>nsub> library. Whereas all polymers assemble into nanoparticles, the bulk mechanical properties of the E<sub>nsub>C are very different from CE<sub>nsub>. The E<sub>nsub>C members demonstrate viscolelastic behavior under ambient conditions and assemble into elastic soft gels above their T<sub>tsub> values. By contrast, the CE<sub>nsub> members are predominantly viscous at all temperatures. All library members demonstrate binding to curcumin. The differential thermoresponsive behaviors of the E<sub>nsub>C and CE<sub>nsub> libraries in addition to their small molecule recognition abilities make them suitable for potential use in tissue engineering and drug delivery.