Synthesis and capping of water-dispersed gold nanoparticles by an amino acid: Bioconjugation and binding studies

• Published in: Journal of colloid and interface science Vol. 323; no. 2; pp. 247 - 254
• Main Authors: Wangoo, Nishima, Bhasin, K.K., Mehta, S.K., Suri, C. Raman
• Format: Journal Article
• Language: English
• Published: San Diego, CA Elsevier Inc 15.07.2008; Elsevier
• Subjects: Amino Acids - chemistry; Bioconjugation; Carboxylic Acids - chemistry; Chemistry; Chlorides - chemistry; Circular Dichroism; Colloidal state and disperse state; Electrophoresis, Agar Gel; Exact sciences and technology; General and physical chemistry; Glutamic acid; Glutamic Acid - chemistry; Gold - chemistry; Gold Compounds - chemistry; Gold nanoparticles; Immunodiagnostic; Light; Metal Nanoparticles - chemistry; Microscopy, Electron, Transmission; Nanotechnology - methods; Physical and chemical studies. Granulometry. Electrokinetic phenomena; Scattering, Radiation; Spectrophotometry, Ultraviolet - methods; Spectroscopy, Fourier Transform Infrared; Surface physical chemistry; Surface Properties; Glutamic acid; Bioconjugation; Immunodiagnostic; Gold nanoparticles; Water; Binding; Gold nanoparticles;Glutamic acid;Bioconjugation;Immunodiagnostic; Gold; Capping; Synthesis; Nanoparticle; Aminoacid; Transition metal
• ISSN: 0021-9797; 1095-7103
• DOI: 10.1016/j.jcis.2008.04.043

We report a novel strategy for the synthesis of aqueous stable, carboxylated gold nanoparticles (GNPs) by using glutamic acid as the reducing agent. The ratio of chloroaurate ions, AuCl − 4 to glutamic acid was optimized in the reaction medium to obtain monodispersed GNPs. Glutamic acid reduced gold nanoparticles were characterized by UV–visible, FTIR, dynamic light scattering and transmission electron microscopy, which demonstrated high stability in aqueous solution over a period of time indicating stabilization via surface-bound amino acid. Functionalized nanoparticles were conjugated with protein molecules through electrostatic attraction between the surface-terminated negatively charged carboxylate groups ( COO −) of glutamic acid and the positively charged amino groups ( NH + 3) of the protein. The conjugation efficiency of the GNP:protein conjugates was confirmed qualitatively and quantitatively through gel electrophoresis and critical flocculation concentration analysis. The interaction between functionalized GNPs with protein molecules was investigated using fluorescence spectroscopy showing the fluorescence quenching of the tryptophan residues of protein molecules after conjugation. Circular dichroism (CD) studies of the conjugates confirmed that the protein undergoes a more flexible conformational state on the boundary surface of GNPs after conjugation. There was substantial conformational transition from α-helix to β-sheet structure after conjugation of protein to GNPs. Reduction of chloroauric acid by glutamic acid results in the formation of aqueous stable and biocompatible gold nanoparticles. Spectroscopic studies of the bioconjugates confirmed the adsorption induced conformational changes in the protein molecules.