A spectroscopic and computational intervention of interaction of lysozyme with 6-mercaptopurine.
Bikash Chandra SwainSandip Kumar MukherjeeJanmejaya Routnull SakshiPadmaja Prasad MishraMandira MukherjeeUmakanta TripathyPublished in: Analytical and bioanalytical chemistry (2020)
In the present work, biophysical insight into the binding interactions of the protein, hen egg white (HEW) lysozyme (Lyz) with an anticancer drug, 6-mercaptopurine (6-MP)' was investigated by using a combination of spectroscopic and computational tools. 6-MP, a synthetic analog of natural purines, is a well-known anticancer drug and antiviral agent that inhibits the synthesis of RNA, DNA, and proteins. Lysozyme is a single-chain protein that can combine with endogenous and exogenous substances to exert its antiviral, antibacterial, and antitumor effects. The intrinsic fluorescence of lysozyme was quenched with the increased addition of 6-MP. The quenching mechanism was found to be static in nature as shown by the fluorescence lifetime and excitation spectrum measurements. The conformational changes of Lyz in the presence of 6-MP were monitored both at the ensemble and single-molecule level by using synchronous fluorescence spectroscopy, circular dichroism (CD), and fluorescence correlation spectroscopy (FCS). Molecular docking results predicted the probable binding sites for 6-MP on Lyz. The experimental findings are in good agreement with the results obtained by the molecular dynamics (MD) simulation study. Graphical abstract.
Keyphrases
- single molecule
- molecular docking
- molecular dynamics
- atomic force microscopy
- living cells
- molecular dynamics simulations
- energy transfer
- density functional theory
- randomized controlled trial
- binding protein
- adverse drug
- quantum dots
- silver nanoparticles
- convolutional neural network
- transcription factor
- deep learning
- solid state