《Spectroscopic and theoretical methods to probe protein-ligand binding》 was published in Materials Today: Proceedings in 2020. These research results belong to Sreedhanya, S.; Jeena, V. R.; Ammu, S.; Aravindakumar, C. T.; Aravind, Usha K.. Synthetic Route of C20H14O The article mentions the following:
Protein-ligand binding studies have gained considerable attention owing to its application in biomedical research. The present study discusses the application of spectroscopic and theor. methods to probe the interaction between a model ligand, 1, 3-diphenylisobenzofuran (DPBF) and bovine serum albumin (BSA). The quenching of the intrinsic fluorescence of BSA arising from tryptophan residue in the presence of DPBF is monitored to follow the nature and mechanism associated with the binding process. The binding affinity and number of binding sites have been investigated. Synchronous fluorescence and UV-Vis spectroscopic studies have been carried out to follow the changes in the fluorophore micro-environment and binding mechanism. Theor. methods such as fluorescence resonance energy transfer (FRET) and mol. docking are also employed to predict the binding mechanism, binding modes, binding sites and the distance between the tryptophan residue in BSA and DPBF. The experimental part of the paper was very detailed, including the reaction process of 1,3-Diphenylisobenzofuran(cas: 5471-63-6Synthetic Route of C20H14O)
1,3-Diphenylisobenzofuran(cas: 5471-63-6) can be used as a fluorescent probe for detection of superoxide anion radical (O2−) inside the membrane lipid layer by DPBF fluorescence quenching method. 1,3-Diphenylisobenzofuran(DPBF) can be used to study the single crystal molecular structure and solution photophysical properties of DPBF.Synthetic Route of C20H14O
Referemce:
Benzofuran – Wikipedia,
Benzofuran | C8H6O – PubChem