Structural studies of amphiphilic 4-helix bundle peptides incorporating designed extended chromophores for nonlinear optical biomolecular materials.
Extended conjugated chromophores containing (porphinato)zinc components that exhibit large optical polarizabilities and hyperpolarizabiliites are incorporated into amphiphilic 4-helix bundle peptides via specific axial histidyl ligation of the metal. The bundle's designed amphiphilicity enables vectorial orientation of the chromophore/peptide complex in macroscopic monolayer ensembles. The 4-helix bundle structure is maintained upon incorporation of two different chromophores at stoichiometries of 1-2 per bundle. The axial ligation site appears to effectively control the position of the chromophore along the length of the bundle.
Strzalka
Joseph
J
Department of Chemistry, University of Pennsylvania, 231 South 34th Street, Philadelphia, Pennsylvania 19104, USA.
Xu
Ting
T
Tronin
Andrey
A
Wu
Sophia P
SP
Miloradovic
Ivan
I
Kuzmenko
Ivan
I
Gog
Thomas
T
Therien
Michael J
MJ
Blasie
J Kent
JK
D001672:Biocompatible Materials / Q000737:chemistry*; D008024:Ligands; D015394:Molecular Structure; D055095:Optics and Photonics; D009942:Organometallic Compounds / Q000737:chemistry*; D010455:Peptides / Q000138:chemical synthesis / Q000737:chemistry*; D011166:Porphyrins / Q000737:chemistry*; D017510:Protein Folding; D017433:Protein Structure, Secondary; D012428:Ruthenium / Q000737:chemistry*; D013329:Structure-Activity Relationship; D013499:Surface Properties; D014961:X-Ray Diffraction; D015032:Zinc / Q000737:chemistry*
D001672:Biocompatible Materials; D008024:Ligands; D009942:Organometallic Compounds; D010455:Peptides; D011166:Porphyrins; D012428:Ruthenium; D015032:Zinc