Amphiphilic four-helix bundle peptides designed for light-induced electron transfer across a soft interface.
A family of four-helix bundle peptides were designed to be amphiphilic, possessing distinct hydrophilic and hydrophobic domains along the length of the bundle's exterior. This facilitates their vectorial insertion across a soft interface between polar and nonpolar media. Their design also now provides for selective incorporation of electron donor and acceptor cofactors within each domain. This allows translation of the designed intramolecular electron transfer along the bundle axis into a macroscopic charge separation across the interface.
Ye
Shixin
S
Department of Chemistry, University of Pennsylvania, Philadelphia, Pennsylvania 19104, USA.
Discher
Bohdana M
BM
Strzalka
Joseph
J
Xu
Ting
T
Wu
Sophia P
SP
Noy
Dror
D
Kuzmenko
Ivan
I
Gog
Thomas
T
Therien
Michael J
MJ
Dutton
P Leslie
PL
Blasie
J Kent
JK
D000595:Amino Acid Sequence; D015195:Drug Design; D004579:Electron Transport; D008958:Models, Molecular; D008969:Molecular Sequence Data; D049329:Nanostructures / Q000737:chemistry*; D036103:Nanotechnology / Q000379:methods*; D010455:Peptides / Q000737:chemistry*; D017433:Protein Structure, Secondary; D055672:Static Electricity; D014961:X-Ray Diffraction
D010455:Peptides