Fluorescence and Aggregation Behavior of Poly(amidoamine) Dendrimers Peripherally Modified with Aromatic Chromophores: the Effect of Dendritic Architectures
Citations Over TimeTop 10% of 2004 papers
Abstract
PAMAM dendrimers of the zeroth to fifth generation (G0-5) have been peripherally modified with phenyl, naphthyl, pyrenyl, and dansyl chromophores. Their fluorescence behaviors are strongly affected by the dendritic architectures at different generations. These dendrimers modified with hydrophobic chromphores can self-organize into vesicular aggregates at the low generations G0-3 in water. The size and aggregation number of these vesicles decrease with increasing generation from G0 to G3. Critical aggregation concentration determined by fluorescence spectroscopy reveals that these aggregates can be favorably formed in the order of G3 > G2 > G1. In contrast to the vesicles made from traditional amphiphilic compounds, these dendrimer-based vesicles are very adhesive due to the H-bonding interaction and entanglement of dendritic branches located in the outer layer. A large number of multivesicle assemblies, i.e., "twins" and "quins" consisting of two and five vesicles, were clearly identifiable with transmission electron (TEM) and atomic force microscopy. For the dendrimers with peripheral pyrenyl chromophores, triangle-like vesicles were observed in water. The hydrophobic interphase thickness of the vesicular bilayer is ca. 2.0-3.2 nm determined by fluorescence resonance energy transfer methods, which agrees well with the thickness directly observed with TEM.
Related Papers
- → Development of homogeneous binding assays based on fluorescence resonance energy transfer between quantum dots and Alexa Fluor fluorophores(2006)64 cited
- → Development of a novel FRET immunosensor technique(2003)49 cited
- → New “X-type” second-order nonlinear optical (NLO) dendrimers: fewer chromophore moieties and high NLO effects(2015)33 cited
- → Bidirectional Fluorescence Resonance Energy Transfer (FRET) in Mutated and Chemically Modified Yellow Fluorescent Protein (YFP)(2011)12 cited