Diffusion and Conformation of Peptide-Functionalized Polyphenylene Dendrimers Studied by Fluorescence Correlation and 13C NMR Spectroscopy

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• 作者：K. Koynov ; G. Mihov ; M. Mondeshki ; C. Moon ; H. W. Spiess ; K. M&uuml ; llen ; H-J. Butt ; G. Floudas
• 刊名：Biomacromolecules
• 出版年：2007
• 出版时间：May 2007
• 年：2007
• 卷：8
• 期：5
• 页码：1745 - 1750
• 全文大小：183K
• 年卷期：v.8,no.5(May 2007)
• ISSN：1526-4602

文摘

We report on the combined use of fluorescence correlation spectroscopy (FCS) and ¹H and ¹³C NMR spectroscopyto detect the size and type of peptide secondary structures in a series of poly-Z-L-lysine functionalized polyphenylenedendrimers bearing the fluorescent perylenediimide core in solution. In dilute solution, the size of the moleculeas detected from FCS and ¹H NMR diffusion measurements matches nicely. We show that FCS is a sensitiveprobe of the core size as well as of the change in the peptide secondary structure. However, FCS is less sensitiveto functionality. A change in the peptide secondary conformation from ages/gifchars/beta2.gif" BORDER=0 ALIGN="middle">-sheets to ages/gifchars/alpha.gif" BORDER=0>-helices detected by ¹³CNMR spectroscopy gives rise to a steep increase in the hydrodynamic radii for number of residues n ages/entities/ge.gif"> 16.Nevertheless, helices are objects of low persistence.