Dieckmann, Gregg R.

Permanent URI for this collectionhttps://hdl.handle.net/10735.1/3994

Gregg Dieckmann is an Associate Professor of Biophysics and Inorganic Chemistry as well as of Bionanotechnology. He is also an affiliated faculty member of the Alan G. MacDiarmid NanoTech Institute. His laboratory uses "protein design to create simple model systems. These systems provide insights into the functioning of more complex biological systems, or yield new bio/nano hybrid materials." His research interests include:

  • Thiolate-rich Zn(II) sites and alkyl transfef
  • Designed protein motifs and carbon nanotubes
  • DNA-binding domains
  • Membrane fusion/protein-protein interactions
Learn more about Dr. Dieckmann here.


Recent Submissions

Now showing 1 - 2 of 2
  • Item
    A Carbon Nanotube-based Raman-imaging Immunoassay For Evaluating Tumor Targeting Ligands
    (Royal Society of Chemistry, 2014-04-16) Bajaj, Pooja; Mikoryak, Carole; Wang, Ruhung; Bushdiecker II, David K.; Memon, Pauras; Draper, Rockford K.; Dieckmann, Gregg R.; Pantano, Paul; Musselman, Inga H.; Pantano, Paul; Musselman, Inga H.
    Herein, we describe a versatile immunoassay that uses biotinylated single-walled carbon nanotubes (SWNTs) as a Raman label, avidin-biotin chemistry to link targeting ligands to the label, and confocal Raman microscopy to image whole cells. Using a breast tumor cell model, we demonstrate the usefulness of the method to assess membrane receptor/ligand systems by evaluating a monoclonal antibody, Her-66, known to target the Her2 receptors that are overexpressed on these cells. We present two-dimensional Raman images of the cellular distribution of the SWNT labels corresponding to the distribution of the Her2 receptors in different focal planes through the cell with validation of the method using immunofluorescence microscopy, demonstrating that the Her-66-SWNT complexes were targeted to Her2 cell receptors.;
  • Item
    Modifying the Electronic Properties of Single-Walled Carbon Nanotubes using Designed Surfactant Peptides
    (2012-05-25) Samarajeewa, D. R.; Dieckmann, Gregg R.; Nielsen, Steven O.; Musselman, Inga H.; Nielsen, Steven O.; Musselman, Inga H.
    The electronic properties of carbon nanotubes can be altered significantly by modifying the nanotube surface. In this study, single-walled carbon nanotubes (SWCNTs) were functionalized noncovalently using designed surfactant peptides, and the resultant SWCNT electronic properties were investigated. These peptides have a common amino acid sequence of X(Valine) 5(Lysine) 2, where X indicates an aromatic amino acid containing either an electron-donating or electron-withdrawing functional group (i.e. p-amino-phenylalanine or p-cyano-phenylalanine). Circular dichroism spectra showed that the surfactant peptides primarily have random coil structures in an aqueous medium, both alone and in the presence of SWCNTs, simplifying analysis of the peptide/SWCNT interaction. The ability of the surfactant peptides to disperse individual SWCNTs in solution was verified using atomic force microscopy and ultraviolet-visible-near-infrared spectroscopy. The electronic properties of the surfactant peptide/SWCNT composites were examined using the observed nanotube Raman tangential band shifts and the observed additional features near the Fermi level in the scanning tunneling spectroscopy dI/dV spectra. The results revealed that SWCNTs functionalized with surfactant peptides containing electron-donor or electron-acceptor functional groups showed n-doped or p-doped altered electronic properties, respectively. This work unveils a facile and versatile approach to modify the intrinsic electronic properties of SWCNTs using a simple peptide structure, which is easily adaptable to obtain peptide/SWCNT composites for the design of tunable nanoscale electronic devices.

Works in Treasures @ UT Dallas are made available exclusively for educational purposes such as research or instruction. Literary rights, including copyright for published works held by the creator(s) or their heirs, or other third parties may apply. All rights are reserved unless otherwise indicated by the copyright owner(s).