A Polymeric Domain That Promotes Cellular Internalization
- 1 April 2008
- journal article
- research article
- Published by American Chemical Society (ACS) in Journal of the American Chemical Society
- Vol. 130 (17) , 5626-5627
- https://doi.org/10.1021/ja8001716
Abstract
Polymers have emerged as powerful biological tools; however, their ability to gain access to the intracellular environment is limited. To expand the biological utility of polymer scaffolds, we have synthesized an internalization domain using the ring-opening metathesis polymerization (ROMP). A polymer functionalized with guanidinium groups is effectively internalized by cells and localized in both vesicles and the cytoplasm. Because the synthesis of such materials is modular, we anticipate that compounds of this type can be fashioned that facilitate the delivery of cargo via end-cap derivatization or block copolymer synthesis.Keywords
This publication has 39 references indexed in Scilit:
- Trivalent Ligands with Rigid DNA Spacers Reveal Structural Requirements For IgE Receptor Signaling in RBL Mast CellsACS Chemical Biology, 2007
- Characterization of the pH of Folate Receptor-Containing Endosomes and the Rate of Hydrolysis of Internalized Acid-Labile Folate-Drug ConjugatesThe Journal of Pharmacology and Experimental Therapeutics, 2007
- Dendritic Molecular Transporters Provide Control of Delivery to Intracellular CompartmentsBioconjugate Chemistry, 2007
- Romping the cellular landscape: linear scaffolds for molecular recognitionCurrent Opinion in Structural Biology, 2006
- Contrast Agents for Magnetic Resonance Imaging Synthesized with Ring-Opening Metathesis PolymerizationJournal of the American Chemical Society, 2006
- Solid-Phase Synthesis of Polymers Using the Ring-Opening Metathesis PolymerizationJournal of the American Chemical Society, 2005
- TAT‐mediated endocytotic delivery of the loop deletion Bcl‐2 protein protects neurons against cell deathJournal of Neurochemistry, 2005
- Pathway for Polyarginine Entry into Mammalian CellsBiochemistry, 2004
- Cell-penetrating PeptidesJournal of Biological Chemistry, 2003
- Arginine-rich PeptidesJournal of Biological Chemistry, 2001