Supramolecular Modification of the Periphery of Dendrimers Resulting in Rigidity and Functionality

Baars, Maurice W. P. L.; Karlsson, Annika J.; Sorokin, V. E.; Waal, Bas F. W. de; Meijer, E. W.

doi:10.1002/1521-3773(20001201)39:23<4262::aid-anie4262>3.0.co;2-y

Cited by 94 publications

(114 citation statements)

References 16 publications

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“…This was later obtained through non-covalent bonding of surface groups. [9,10] (1992). He has since worked with immunology and protein chemistry in various projects at the borderline between bioorganic chemistry and infection biology at the University of Copenhagen, in the private sector, and, presently, at the National Veterinary Institute (Technical University of Denmark) in Copenhagen.…”

Section: Feature Articlementioning

confidence: 99%

Dendrimer Effects on Peptide and Protein Fibrillation

Heegaard

Boas

Otzen

2007

Macromolecular Bioscience

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Dendrimers are synthetic, symmetrically branched polymers that can be manufactured to a high degree of definition and therefore present themselves as monodisperse entities. Flexible and globular in shape and compartementalized into a partly inaccessible interior and a highly exposed surface, they offer numerous possibilities for interactions with and responses to biological macromolecules and biostructures including cell membranes and proteins. By way of their multiple functional surface groups, they allow the design of surfaces carrying a multitude of biological motifs and/or charges giving rise to quite significant biological and physico-chemical effects. Here we describe the surprising ability of dendrimers to interact with and perturb polypeptide conformations, particularly efficiently towards amyloid structures; that is, the structures of highly insoluble polypeptide aggregates involved in a range of serious and irreversibly progressive pathological conditions (protein-misfolding diseases). Interesting as this may be, the interaction of dendrimers with such generic peptidic aggregates also offers a new perspective on the molecular mechanisms governing assembly and disassembly of amyloid structures and thereby on determinants of protein and peptide folding. Despite the potent disaggregative nature of various dendrimers, they have variable effects on the stability of different proteins, suggesting that they do not act as generic denaturants, but rather exert their effects via specific interactions with individual parts of each protein.

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Section: Feature Articlementioning

confidence: 99%

Dendrimer Effects on Peptide and Protein Fibrillation

Heegaard

Boas

Otzen

2007

Macromolecular Bioscience

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“…11). To this end, we have used the fifth-generation poly(propylene imine) dendrimer functionalized with urea adamantyl units at the periphery (31) [52] that allows the non-covalent anchoring of phosphine ligands with the complementary binding motive [53] (Fig. 12).…”

Section: Non-covalently Functionalized Dendrimers As Recyclable Catalmentioning

confidence: 99%

Phosphine-functionalized dendrimers for transition-metal catalysis

Reek

Groot

Oosterom

et al. 2003

Comptes Rendus. Chimie

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“…IR: 3310 (NH 2 ), 2903, 2848, 2800 (CH, CH 2 ), 1636 (CO), 1558 cm −1 (N−H, NH 2 ). NMR data of fully adamantyl-substituted PPI-G3 dendrimers were reported by Baars et al in ref 43.…”

Section: Firstmentioning

confidence: 89%

Supramolecular Glycodendrimer-Based Hybrid Drugs

Paolino

Komber

Mennuni³

et al. 2014

Biomacromolecules

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Specific noncovalent interactions are commonly used by nature to modulate numerous processes including cell recognition, viral adhesion, and transmembrane communications. Here we report on the design, synthesis, and preliminary characterization of new supramolecular glycodendrimer-based hybrid drugs based on adamantyl-modified glycodendrimers of third, fourth, or fifth generation (mPPI-G3-AdaB, mPPI-G4-AdaB, and mPPI-G5-AdaB) and a new heterobifunctional ligand. This component was tailored to bind through noncovalent interactions both the multimeric natural 5-HT3 receptor (through an optimized arylpiperazine pharmacophore) and the adamantyl groups located on the glycodendrimer surfaces (through a β-cyclodextrin residue) giving rise to biorelevant supramolecular constructs.

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Supramolecular Modification of the Periphery of Dendrimers Resulting in Rigidity and Functionality

Cited by 94 publications

References 16 publications

Dendrimer Effects on Peptide and Protein Fibrillation

Dendrimer Effects on Peptide and Protein Fibrillation

Phosphine-functionalized dendrimers for transition-metal catalysis

Supramolecular Glycodendrimer-Based Hybrid Drugs

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