Micelle Density Regulated by a Reversible Switch of Protein Secondary Structure

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• 作者：Rory E. Sallach ; Min Wei ; Nilanjana Biswas ; Vincent P. Conticello ; Sé ; bastien Lecommandoux ; Richard A. Dluhy ; Elliot L. Chaikof
• 刊名：Journal of the American Chemical Society
• 出版年：2006
• 出版时间：September 13, 2006
• 年：2006
• 卷：128
• 期：36
• 页码：12014 - 12019
• 全文大小：367K
• 年卷期：v.128,no.36(September 13, 2006)
• ISSN：1520-5126

文摘

Protein secondary structures may exhibit reversible transitions that occur in an abrupt andcontrollable manner. In this report, we demonstrate that such transitions may be utilized in the design ofa "smart" protein micellar system, in which a stimulus-induced change in protein structure triggers a rapidchange in micelle compacticity and size. Specifically, recombinant DNA methods were used to prepare aprotein triblock copolymer containing a central hydrophilic block and two hydrophobic end blocks derivedfrom elastin-mimetic peptide sequences. Below the copolymer inverse transition temperature (T_t), dilutesolutions of this amphiphilic protein formed monodispersed micelles in a narrow range of R_H of ~100 nm.When the the temperature was raised above T_t, an abrupt increase in micelle internal density was observedwith a concomitant reduction in micelle size. This reversible change in micelle compacticity was triggeredby helix-to-sheet protein folding transition. Significantly, these protein polymer-based micelles, which arerapidly responsive to environmental stimuli, establish a new mechanism for the design of controlled drugdelivery vehicles.