Mathematical modeling of interactions of cabergoline with human serum albumin for biosensing of human serum albumin
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چکیده
منابع مشابه
Fluoxetin Competes with Cortisol for Binding to Human Serum Albumin
Human serum albumin (HSA) is an important protein that carries variety of substances like some hormones and drugs in blood. Pharmacological studies of the interaction of many drugs and HSA are reported during several decades, specially recently years. Interaction of cortisol and fluoxetine hydrochloride (FLX) (as a common anti-stress drug) with HSA (as their carrier in blood) has been studied s...
متن کاملFluoxetin Competes with Cortisol for Binding to Human Serum Albumin
Human serum albumin (HSA) is an important protein that carries variety of substances like some hormones and drugs in blood. Pharmacological studies of the interaction of many drugs and HSA are reported during several decades, specially recently years. Interaction of cortisol and fluoxetine hydrochloride (FLX) (as a common anti-stress drug) with HSA (as their carrier in blood) has been studied s...
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Background and Aims: Some nanoparticles can be used in immunoassays to increase sensitivity. This study aimed to evaluate a novel nano-immunoassay based on bovine serum albumin nanoparticles (BSA NPs). Materials and methods: At first, the nanostructure was synthesized, and then applied as a tag in the nano-immunoassay. Then the concentration of β-subunit of human chorionic gonadotropin ...
متن کاملThe Effects of Acetaminophen on Human Serum Albumin (HSA)
Thermal conformational changes in human serum albumin (HSA) in present with a 10 mM phosphate buffer, at pH=7 have been investigated via circular dichroism (CD) and UV spectroscopic methods. The results indicate that temperature in a range of 25oC to 55oC could induce a reversible conformational change in the structure of HSA. The HSA phase transition corresponds to the physiological and patho...
متن کاملThe Effects of Acetaminophen on Human Serum Albumin (HSA)
Thermal conformational changes in human serum albumin (HSA) in present with a 10 mM phosphate buffer, at pH=7 have been investigated via circular dichroism (CD) and UV spectroscopic methods. The results indicate that temperature in a range of 25oC to 55oC could induce a reversible conformational change in the structure of HSA. The HSA phase transition corresponds to the physiological and patho...
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ژورنال
عنوان ژورنال: Sensing and Bio-Sensing Research
سال: 2019
ISSN: 2214-1804
DOI: 10.1016/j.sbsr.2019.100297