Micelle density regulated by a reversible switch of protein secondary structure
LECOMMANDOUX, Sebastien
Laboratoire de Chimie des polymères organiques [LCPO]
Team 3 LCPO : Polymer Self-Assembly & Life Sciences
Laboratoire de Chimie des polymères organiques [LCPO]
Team 3 LCPO : Polymer Self-Assembly & Life Sciences
CHAIKOF, Elliot L.
Department of Biomedical Engineering [Atlanta]
Lab Biomol Mat Res [Emory Univ]
Georgia Inst Technol, Sch Chem & Biomol Engn
< Réduire
Department of Biomedical Engineering [Atlanta]
Lab Biomol Mat Res [Emory Univ]
Georgia Inst Technol, Sch Chem & Biomol Engn
Langue
en
Article de revue
Ce document a été publié dans
Journal of the American Chemical Society. 2006, vol. 128, n° 36, p. 12014-12019
American Chemical Society
Résumé en anglais
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 ...Lire la suite >
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 (T-t), dilute solutions of this amphiphilic protein formed monodispersed micelles in a narrow range of R-H of similar to 100 nm. When the the temperature was raised above T-t, 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.< Réduire
Mots clés en anglais
copolymer
conformation
beta-sheet
elastin
inverse temperature transition
LCST
protein
alpha-helix
Origine
Importé de halUnités de recherche