Micelle density regulated by a reversible switch of protein secondary structure

Academic Article

Abstract

  • Protein secondary structures may exhibit reversible transitions that occur in an abrupt and controllable manner. In this report, we demonstrate that such transitions may be utilized in the design of a "smart" protein micellar system, in which a stimulus-induced change in protein structure triggers a rapid change in micelle compacticity and size. Specifically, recombinant DNA methods were used to prepare a protein triblock copolymer containing a central hydrophilic block and two hydrophobic end blocks derived from elastin-mimetic peptide sequences. Below the copolymer inverse transition temperature (Tt), dilute solutions of this amphiphilic protein formed monodispersed micelles in a narrow range of RH of ∼100 nm. When the the temperature was raised above Tt, an abrupt increase in micelle internal density was observed with a concomitant reduction in micelle size. This reversible change in micelle compacticity was triggered by helix-to-sheet protein folding transition. Significantly, these protein polymer-based micelles, which are rapidly responsive to environmental stimuli, establish a new mechanism for the design of controlled drug delivery vehicles. © 2006 American Chemical Society.
  • Authors

    Digital Object Identifier (doi)

    Pubmed Id

  • 22031865
  • Author List

  • Sallach RE; Wei M; Biswas N; Conticello VP; Lecommandoux S; Dluhy RA; Chaikof EL
  • Start Page

  • 12014
  • End Page

  • 12019
  • Volume

  • 128
  • Issue

  • 36