NIR-II-Absorbing TMB Derivative for 1064 nm-Excited Photothermal Immunoassay.

Materials exhibiting strong absorption in the NIR-II region are appealing for photothermal conversion-based imaging, diagnosis, and therapy, due to better thermal effect and decreased absorption of water in such a region. 3,3',5,5'-Tetramethylbenzidine (TMB), the typical substrate in ELISA, has been explored in photothermal immunoassay, since its oxidation product (oxTMB) is photothermally active in the NIR region. However, its absorption at 1064 nm (the most often used laser wavelength in photothermal studies) is not appreciable, thus limiting the assay sensitivity.

Investigation on the interaction between myricetin and dihydromyricetin with trypsin, α-chymotrypsin, lysozyme by spectroscopy and molecular docking methods.

The interaction between myricetin and dihydromyricetin with trypsin, α-chymotrypsin and lysozyme was investigated using multispectral and molecular docking methods. The results of fluorescence quenching revealed that myricetin and dihydromyricetin could quench the intrinsic fluorescence of three different proteinases through a static quenching procedure. The binding constant and number of binding sites at different temperatures were measured.

Study on the interaction between nimodipine and five proteinases and the effects of naringin and vitamin C on these interactions by spectroscopic and molecular docking methods.

The interaction mechanisms of nimodipine with pepsin, trypsin, α-chymotrypsin, lysozyme and human serum albumin were investigated by multispectral and molecular docking methods. Vitamin C and naringin were the main active components of grapefruit juice, and nimodipine was the typical drug that interacts with this juice. Fluorescence spectroscopy was used to study the interaction of nimodipine with five proteinases (pepsin, trypsin, α-chymotrypsin, lysozyme and human serum albumin) and the effects of vitamin C and naringin on these interactions.

Structural and emulsifying properties of soybean protein isolate glycated with glucose based on pH treatment.

Backgrounds: In the present study, a glycosylated soybean protein with glucose was prepared after pH treatment under different conditions (5.0, 6.0 7.