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Bioactivation and cell targeting of semiconductor CdSe/ZnS nanocrystals with phytochelatin-related peptides.


ABSTRACT: Synthetic phytochelatin-related peptides are used as an organic coat on the surface of colloidal CdSe/ZnS semiconductor nanocrystals synthesized from hydrophobic coordinating trioctyl phosphine oxide (TOPO) solvents. The peptides are designed to bind to the nanocrystals via a C-terminal adhesive domain. This adhesive domain, composed of multiple repeats of cysteines pairs flanked by hydrophobic 3-cyclohexylalanines, is followed by a flexible hydrophilic linker domain to which various bio-affinity tags can be attached. This surface coating chemistry results in small, buffer soluble, monodisperse peptide-coated nanoparticles with high colloidal stability and ensemble photophysical properties similar to those of TOPO-coated nanocrystals. Various peptide coatings are used to modulate the nanocrystal surface properties and to bioactivate the nanoparticles. CdSe/ZnS nanocrystals coated with biotinylated peptides efficiently bind to streptavidin and are specifically targeted to GPI-anchored avidin-CD14 chimeric proteins expressed on the membranes of live HeLa cells. This peptide coating surface chemistry provides a novel approach for the production of biocompatible photoluminescent nanocrystal probes.

SUBMITTER: Pinaud F 

PROVIDER: S-EPMC5715196 | biostudies-literature | 2004 May

REPOSITORIES: biostudies-literature

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Bioactivation and cell targeting of semiconductor CdSe/ZnS nanocrystals with phytochelatin-related peptides.

Pinaud Fabien F   King David D   Moore Hsiao-Ping HP   Weiss Shimon S  

Journal of the American Chemical Society 20040501 19


Synthetic phytochelatin-related peptides are used as an organic coat on the surface of colloidal CdSe/ZnS semiconductor nanocrystals synthesized from hydrophobic coordinating trioctyl phosphine oxide (TOPO) solvents. The peptides are designed to bind to the nanocrystals via a C-terminal adhesive domain. This adhesive domain, composed of multiple repeats of cysteines pairs flanked by hydrophobic 3-cyclohexylalanines, is followed by a flexible hydrophilic linker domain to which various bio-affinit  ...[more]

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