@article{tkachenko_xie_liu_coleman_ryan_glomm_shipton_franzen_feldheim_2004, title={Cellular trajectories of peptide-modified gold particle complexes: Comparison of nuclear localization signals and peptide transduction domains}, volume={15}, ISSN={["1520-4812"]}, DOI={10.1021/bc034189q}, abstractNote={Gold nanoparticles modified with nuclear localization peptides were synthesized and evaluated for their subcellular distribution in HeLa human cervical epithelium cells, 3T3/NIH murine fibroblastoma cells, and HepG2 human hepatocarcinoma cells. Video-enhanced color differential interference contrast microscopy and transmission electron microscopy indicated that transport of nanoparticles into the cytoplasm and nucleus depends on peptide sequence and cell line. Recently, the ability of certain peptides, called protein transduction domains (PTDs), to transclocate cell and nuclear membranes in a receptor- and temperature-independent manner has been questioned (see for example, Lundberg, M.; Wikstrom, S.; Johansson, M. (2003) Mol. Ther. 8, 143-150). We have evaluated the cellular trajectory of gold nanoparticles carrying the PTD from HIV Tat protein. Our observations were that (1) the conjugates did not enter the nucleus of 3T3/NIH or HepG2 cells, and (2) cellular uptake of Tat PTD peptide-gold nanoparticle conjugates was temperature dependent, suggesting an endosomal pathway of uptake. Gold nanoparticles modified with the adenovirus nuclear localization signal and the integrin binding domain also entered cells via an energy-dependent mechanism, but in contrast to the Tat PTD, these signals triggered nuclear uptake of nanoparticles in HeLa and HepG2 cell lines.}, number={3}, journal={BIOCONJUGATE CHEMISTRY}, author={Tkachenko, AG and Xie, H and Liu, YL and Coleman, D and Ryan, J and Glomm, WR and Shipton, MK and Franzen, S and Feldheim, DL}, year={2004}, pages={482–490} }
 @article{kramer_xie_gaff_williamson_tkachenko_nouri_feldheim_feldheim_2004, title={Preparation of protein gradients through the controlled deposition of protein-nanoparticle conjugates onto functionalized surfaces}, volume={126}, ISSN={["0002-7863"]}, DOI={10.1021/ja031674n}, abstractNote={This paper describes a simple method for the preparation and characterization of protein density gradients on solid supports. The method employs colloidal metal nanoparticles as protein carriers and optical tags and is capable of forming linear, exponential, 1D, 2D, and multiprotein gradients of varying slope without expensive or sophisticated surface patterning techniques. Surfaces patterned with proteins using the procedures described within are shown to support cell growth and are thus suitable for studies of protein−cell interactions.}, number={17}, journal={JOURNAL OF THE AMERICAN CHEMICAL SOCIETY}, author={Kramer, S and Xie, H and Gaff, J and Williamson, JR and Tkachenko, AG and Nouri, N and Feldheim, DA and Feldheim, DL}, year={2004}, month={May}, pages={5388–5395} }
 @article{xie_tkachenko_glomm_ryan_brennaman_papanikolas_franzen_feldheim_2003, title={Critical flocculation concentrations, binding isotherms, and ligand exchange properties of peptide-modified gold nanoparticles studied by UV-visible, fluorescence, and time-correlated single photon counting spectroscopies}, volume={75}, ISSN={["0003-2700"]}, DOI={10.1021/ac034578d}, abstractNote={Protocols for modifying gold nanoparticles with peptide−bovine serum albumin (BSA) conjugates are described within. The resulting constructs were characterized using a number of techniques including static fluorescence spectroscopy and time-correlated single photon counting spectroscopy (TCSPC) in order to quantify peptide−BSA binding isotherms, exchange rates, critical flocculation concentrations, and the composition of mixed peptide−BSA monolayers on gold nanoparticles. TCSPC has proven to be a powerful technique for observing the microenvironment of protein−gold nanoparticle conjugates because it can distinguish between surface-bound and solution-phase species without the need for separation steps. Full characterization of the composition and stability of peptide-modified metal nanoparticles is an important step in their use as intracellular delivery vectors and imaging agents.}, number={21}, journal={ANALYTICAL CHEMISTRY}, author={Xie, H and Tkachenko, AG and Glomm, WR and Ryan, JA and Brennaman, MK and Papanikolas, JM and Franzen, S and Feldheim, DL}, year={2003}, month={Nov}, pages={5797–5805} }