Probing the binding of trypsin to glutathione-stabilized gold nanoparticles in aqueous solution

• Published in: Colloids and surfaces, B, Biointerfaces Vol. 135; pp. 261 - 266
• Main Authors: Wang, Gongke, Liu, Xingbing, Yan, Changling, Bai, Guangyue, Lu, Yan
• Format: Journal Article
• Language: English
• Published: Netherlands Elsevier B.V 01.11.2015
• Subjects: Agglomeration; Au nanoparticles; Binding; Constants; Cooperative binding; Fluorescence; Fluorescence quenching; Glutathione - chemistry; Gold; Gold - chemistry; Interaction; Metal Nanoparticles - chemistry; Nanoparticles; Protein Binding; Protein Conformation; Solutions; Thermodynamics; Trypsin; Trypsin - chemistry; Ultraviolet; Water; Au nanoparticles; Trypsin; Cooperative binding; Interaction; Fluorescence quenching
• ISSN: 0927-7765; 1873-4367
• DOI: 10.1016/j.colsurfb.2015.07.063

We investigate the interaction of trypsin with glutathione-stabilized Au nanoparticles (NPs) using fluorescence, synchronous fluorescence and ultraviolet (UV) absorption spectroscopy. We find that trypsin binds strongly to the Au NPs with a static quenching mechanism, and that the interaction is characteristic of positive cooperative binding. Furthermore, we determine the binding constants and the thermodynamic parameters, which suggest that the main binding forces between the glutathione-stabilized Au NPs and trypsin are electrostatic interactions and hydrogen bonding. Analysis of UV–vis absorption spectra suggests that aggregation of the Au NPs occurs in the trypsin/Au NPs system, which significantly alters the conformation of the protein.