研究目的
Investigating the in vitro interactions of Famotidine and Tapentadol hydrochloride with bovine serum albumin using fluorescence emission spectroscopy.
研究成果
The study concluded that Famotidine and Tapentadol hydrochloride interact with bovine serum albumin, with binding ratios varying with temperature. The interactions were characterized by dynamic quenching, and the binding process was found to be spontaneous with hydrophobic interactions playing a significant role.
研究不足
The study is limited to in vitro conditions and may not fully represent in vivo interactions. The use of BSA, while homologous to HSA, may not perfectly mimic human serum albumin interactions.
1：Experimental Design and Method Selection:
Fluorescence emission spectroscopy was used to study the interactions under different conditions. Quenching constants were determined using the Stern-Volmer equation.
2：Sample Selection and Data Sources:
Bovine serum albumin (BSA) was used due to its 76% sequence homology to human serum albumin (HSA).
3：List of Experimental Equipment and Materials:
F-7000 spectrophotometer (Hitachi, Japan) equipped with 1.0 cm quartz cell and a thermostatic water bath (Unitronic Orbital, P Spectra, Spain) were used.
4：0 cm quartz cell and a thermostatic water bath (Unitronic Orbital, P Spectra, Spain) were used.
Experimental Procedures and Operational Workflow:
4. Experimental Procedures and Operational Workflow: Five mL of 20 μM BSA solution was taken in each of the eight test tubes. FT was added in different volumes to seven out of eight test tubes to have varying concentrations. The systems were stirred for 2 min and kept for 25 min at 298 K and 308 K, respectively.
5：Data Analysis Methods:
The fluorescence intensity of the system at 298 K and 308 K and at the excitation wavelength of 280 nm and 293 nm were estimated. The emission spectra for all systems were recorded in the range of 320-460 nm for BSA at same experimental conditions.
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