11-mercaptoundecanoic-acid and sodium-borohydride

A common capping agent for gold nanorods, Cetyl trimethylammonium bromide (CTAB), is particularly problematic for biological studies because of its cytotoxicity. Several procedures have been developed to remove the CTAB from the surface of the gold nanorods, but most are lengthy, involving many steps, and use expensive reagents. Here, we present a simple, one-pot method for the complete removal of CTAB from the surface of gold nanorods, so that particles can be more effectively utilized in biological in vivo studies. The procedure involves first adding sodium borohydride to remove the CTAB, quickly followed by a replacement ligand, such as mercaptoundecanoic acid (MUA). Both the CTAB removal and MUA replacement were monitored by FTIR, surface enhanced Raman spectroscopy (SERS) and X-Ray Photoelectron Spectroscopy (XPS) and compared to commercially available citrate-capped gold nanorods. The procedure presented herein is shown to be as effective at removing CTAB and replacing it with MUA as commercially available gold nanorod samples.

Topics: Borohydrides; Cetrimonium; Cetrimonium Compounds; Fatty Acids; Gold; Kinetics; Metal Nanoparticles; Nanotubes; Spectroscopy, Fourier Transform Infrared; Sulfhydryl Compounds; Surface Plasmon Resonance; Surface Properties; Thermodynamics

We have conjugated chloroquine, an anti-malarial, antiviral and anti-tumor drug, with thiol-functionalized gold nanoparticles and studied their binding interaction with bovine serum albumin (BSA) protein. Gold nanoparticles have been synthesized using sodium borohydride as reducing agent and 11-mercaptoundecanoic acid as thiol functionalizing ligand in aqueous medium. The formation of gold nanoparticles was confirmed from the characteristic surface plasmon absorption band at 522 nm and transmission electron microscopy revealed the average particle size to be ~7 nm. Chloroquine was conjugated to thiolated gold nanoparticles by using EDC/NHS chemistry and the binding was analyzed using optical density measurement and Fourier transform infrared spectroscopy. The chloroquine-conjugated gold nanoparticles (GNP-Chl) were found to interact efficiently with BSA. Thermodynamic parameters suggest that the binding is driven by both enthalpy and entropy, accompanied with only a minor alteration in protein's structure. Competitive drug binding assay revealed that the GNP-Chl bind at warfarin binding site I in subdomain IIA of BSA and was further supported by Trp212 fluorescence quenching measurements. Unraveling the nature of interactions of GNP-Chl with BSA would pave the way for the design of nanotherapeutic agents with improved functionality, enriching the field of nanomedicine.

Topics: Animals; Antimalarials; Binding Sites; Borohydrides; Cattle; Chloroquine; Fatty Acids; Gold; Microscopy, Electron, Transmission; Models, Molecular; Nanoparticles; Particle Size; Protein Binding; Protein Structure, Tertiary; Serum Albumin, Bovine; Spectroscopy, Fourier Transform Infrared; Sulfhydryl Compounds; Thermodynamics; Tryptophan; Warfarin