Diffusion and conformation of peptide-functionalized polyphenylene dendrimers studied by fluorescence correlation and 13C NMR spectroscopy.
We report on the combined use of fluorescence correlation spectroscopy (FCS) and 1H and 13C NMR spectroscopy to detect the size and type of peptide secondary structures in a series of poly-Z-L-lysine functionalized polyphenylene dendrimers bearing the fluorescent perylenediimide core in solution. In dilute solution, the size of the molecule as detected from FCS and 1H NMR diffusion measurements matches nicely. We show that FCS is a sensitive probe of the core size as well as of the change in the peptide secondary structure. However, FCS is less sensitive to functionality. A change in the peptide secondary conformation from beta-sheets to alpha-helices detected by 13C NMR spectroscopy gives rise to a steep increase in the hydrodynamic radii for number of residues n > or = 16. Nevertheless, helices are objects of low persistence.
Koynov
K
K
Max-Planck-Institut für Polymerforschung, D-55021 Mainz, Germany.
Mihov
G
G
Mondeshki
M
M
Moon
C
C
Spiess
H W
HW
Müllen
K
K
Butt
H-J
HJ
Floudas
G
G
D002247:Carbon Isotopes / Q000032:analysis; D050091:Dendrimers / Q000737:chemistry*; D004058:Diffusion; D005453:Fluorescence; D009682:Magnetic Resonance Spectroscopy / Q000379:methods*; D010455:Peptides / Q000737:chemistry*; D011108:Polymers / Q000737:chemistry*; D017433:Protein Structure, Secondary; D013050:Spectrometry, Fluorescence / Q000379:methods*
D002247:Carbon Isotopes; D050091:Dendrimers; D010455:Peptides; D011108:Polymers; C041325:polyphenylene sulfide