Diffusion and conformation of peptide-functionalized polyphenylene dendrimers studied by fluorescence correlation and C-13 NMR spectroscopy
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Koynov, K.
Mihov, G.
Mondeshki, M.
Moon, C.
Spiess, H. W.
Mullen, K.
Butt, H. J.
Floudas, G.
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peer reviewed
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Biomacromolecules
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We report on the combined use of fluorescence correlation spectroscopy (FCS) and H-1 and C-13 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 H-1 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 C-13 NMR spectroscopy gives rise to a steep increase in the hydrodynamic radii for number of residues n >= 16. Nevertheless, helices are objects of low persistence.
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solid-state nmr, dynamics, diagnostics, stability, polymers
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<Go to ISI>://000246413600047
http://pubs.acs.org/doi/abs/10.1021/bm0702760
http://pubs.acs.org/doi/abs/10.1021/bm0702760
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en
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Πανεπιστήμιο Ιωαννίνων. Σχολή Επιστημών και Τεχνολογιών. Τμήμα Βιολογικών Εφαρμογών και Τεχνολογιών