Study on the Interaction between Stevenleaf and Human Serum Albumin by Fluorescence Spectroscopy
Fei Xu
Abstract
Fei Xu
Abstract
The interaction between stevenleaf and human serum albumin(HSA) in buffer solution(pH=7.40) were studied by fluorescence spectroscopy.It was found that Stevenleaf quenched the fluorescence of HSA via a dynamic quenching process.The binding constant and number of binding sites were found.Values of thermodynamic parameters were calculated.These dates indicated that hydrophobic played a major role in the binding of Stevenleaf and HSA.Synchronous fluorescence spectroscopy was used in the study of the effect of Stevenleaf on the configuration of HSA.
A significance statement is not available in the OpenAlex record.
A contribution statement is not available in the OpenAlex record.
Method details are not available in the OpenAlex metadata.
Findings are not separately available in the OpenAlex metadata.
Limitations are not available in the OpenAlex metadata.
Application details are not available in the OpenAlex metadata.
The interaction between stevenleaf and human serum albumin(HSA) in buffer solution(pH=7.40) were studied by fluorescence spectroscopy.It was found that Stevenleaf quenched the fluorescence of HSA via a dynamic quenching process.The binding constant and number of binding sites were found.Values of thermodynamic parameters were calculated.These dates indicated that hydrophobic played a major role in the binding of Stevenleaf and HSA.Synchronous fluorescence spectroscopy was used in the study of the effect of Stevenleaf on the configuration of HSA.
Key concepts: Human serum albumin, Fluorescence spectroscopy, Fluorescence, Quenching (fluorescence), Spectroscopy, Chemistry, Binding constant, Analytical Chemistry (journal)