Scripps VIVO scripps research logo

  • Index
  • Log in
  • Home
  • People
  • Organizations
  • Research
  • Events
Search form

Interactions between redox complexes and semiconductor quantum dots coupled via a peptide bridge

Academic Article
uri icon
  • Overview
  • Identity
  • Additional Document Info
  • View All
scroll to property group menus

Overview

authors

  • Medintz, I. L.
  • Pons, T.
  • Trammell, S. A.
  • Grimes, A. F.
  • English, D. S.
  • Blanco-Canosa, J. B.
  • Dawson, Philip
  • Mattoussi, H.

publication date

  • 2008

journal

  • Journal of the American Chemical Society  Journal

abstract

  • Colloidal quantum dots (QDs) have a large fraction of their atoms arrayed on their surfaces and are capped with bifunctional ligands, which make their photoluminescence highly sensitive to potential charge transfer to or from the surrounding environment. In this report, we used peptides as bridges between CdSe-ZnS QDs and metal complexes to promote charge transfer between the metal complexes and QDs. We found that quenching of the QD emission is highly dependent on the relative position of the oxidation levels of QDs and metal complex used; it also traces the number of metal complexes brought in close proximity of the nanocrystal surface. In addition, partial bleaching of the absorption was measured for the QD-metal complex assemblies. These proximity driven interactions were further used to construct sensing assemblies to detect proteolytic enzyme activity.

subject areas

  • Absorption
  • Cadmium Compounds
  • Electrochemistry
  • Electron Transport
  • Fluorescence Resonance Energy Transfer
  • Histidine
  • Ligands
  • Luminescence
  • Organometallic Compounds
  • Oxidation-Reduction
  • Peptides
  • Quantum Dots
  • Selenium Compounds
  • Semiconductors
  • Serine Endopeptidases
  • Sulfides
  • Surface Properties
  • Zinc Compounds
scroll to property group menus

Identity

PubMed Central ID

  • PMC2779033

International Standard Serial Number (ISSN)

  • 0002-7863

Digital Object Identifier (DOI)

  • 10.1021/ja805456x

PubMed ID

  • 19049466
scroll to property group menus

Additional Document Info

start page

  • 16745

end page

  • 16756

volume

  • 130

issue

  • 49

©2019 The Scripps Research Institute | Terms of Use | Powered by VIVO

  • About
  • Contact Us
  • Support