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Conformational Analysis of Triazine Dendrimers: Using NMR Spectroscopy To Probe the Choreography of a Dendrimer's Dance.


ABSTRACT: One-dimensional (1D) and two-dimensional (2D) NMR studies are used to probe the conformation of a melamine dendrimer bearing unique NMR signals from the core to the periphery. Four conceptual anchors for dendrimer conformation emerge from these experiments. First, changes in isomer populations observed by (1)H NMR reveal the onset of globular structure. Second, NOE complexity emerges with globular structure: variable temperature NOESY studies show that the peripheral groups, BOC-protected aliphatic amines, fold back into the globular core of the macromolecule at 75 degrees C in DMSO-d(6). Third, variable temperature coefficients measured for NH protons suggest that solvent is largely excluded from the interior of the dendrimer: the carbamate NH groups of the periphery are most sensitive to temperature while the NHs nearest the core show little temperature dependence. Conformation is influenced by solvent choice: backfolding is observed in DMSO-d(6), but not in either CDCl(3) or CD(3)OD. Finally, relaxation studies show that peripheral groups are more dynamic than groups at the core. These anchors consolidate observations made by many groups on disparate systems within a common architecture.

SUBMITTER: Moreno KX 

PROVIDER: S-EPMC2782416 | biostudies-literature | 2008 Jun

REPOSITORIES: biostudies-literature

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Conformational Analysis of Triazine Dendrimers: Using NMR Spectroscopy To Probe the Choreography of a Dendrimer's Dance.

Moreno Karlos X KX   Simanek Eric E EE  

Macromolecules 20080601 12


One-dimensional (1D) and two-dimensional (2D) NMR studies are used to probe the conformation of a melamine dendrimer bearing unique NMR signals from the core to the periphery. Four conceptual anchors for dendrimer conformation emerge from these experiments. First, changes in isomer populations observed by (1)H NMR reveal the onset of globular structure. Second, NOE complexity emerges with globular structure: variable temperature NOESY studies show that the peripheral groups, BOC-protected alipha  ...[more]

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