Micelle density regulated by a reversible switch of protein secondary structure.
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 approximately 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.
Sallach
Rory E
RE
Department of Biomedical Engineering, Georgia Institute of Technology, Atlanta, Georgia 30332, USA.
Wei
Min
M
Biswas
Nilanjana
N
Conticello
Vincent P
VP
Lecommandoux
Sébastien
S
Dluhy
Richard A
RA
Chaikof
Elliot L
EL
D000595:Amino Acid Sequence; D040761:Biomimetic Materials / Q000737:chemistry; D002942:Circular Dichroism; D004549:Elastin / Q000737:chemistry*; D008027:Light; D008823:Micelles; D008969:Molecular Sequence Data; D010455:Peptides / Q000737:chemistry*; D017433:Protein Structure, Secondary; D011994:Recombinant Proteins / Q000737:chemistry; D012542:Scattering, Radiation
D008823:Micelles; D010455:Peptides; D011994:Recombinant Proteins; D004549:Elastin