Mechanism of gold nanoparticles-induced trypsin inhibition: a multi-technique approach.
The binding interactions of gold nanoparticles with trypsin were investigated using multi-spectra methods and molecular modeling. The experiment data showed that trypsin modified the surface of gold nanoparticles. The fluorescence intensity of trypsin was quenched by gold nanoparticles that strongly associated with protein and induced the inhibition of enzyme activity. The electrostatic and hydrophobic interactions were the primary contributors to the binding forces between trypsin and gold nanoparticles. The covalent interactions might be also involved in the binding process. The modeling calculated results indicated that the binding site was near to the primary substrate-binding pocket and the active site of the enzyme substrate. This work elucidated the interaction mechanism of trypsin with gold nanoparticles from the theoretical and experimental angle.
Institute of Applied Chemistry and Environmental Engineering, Yancheng Teachers University, Yancheng, 224002, Jiangsu, People's Republic of China.
Hongmei
H
Zhang
Jian
J
Cao
Shengde
S
Wu
Yanqing
Y
Wang
D001665:Binding Sites / Q000502:physiology; D005453:Fluorescence; D006046:Gold / Q000737:chemistry*; D057927:Hydrophobic and Hydrophilic Interactions; D053768:Metal Nanoparticles / Q000737:chemistry*; D008958:Models, Molecular; D013056:Spectrophotometry, Ultraviolet; D055672:Static Electricity; D013816:Thermodynamics; D014361:Trypsin Inhibitors / Q000737:chemistry*
D014361:Trypsin Inhibitors; D006046:Gold