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Study on the interaction of La with bovine serum albumin at molecular level |
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| Authors: | Dong Yuan Zhonglan Shen Rutao Liu Canzhu Gao |
| Institution: | a Shandong Key Laboratory of Water Pollution Control and Resource Reuse, School of Environmental Science and Engineering, Shandong University, Jinan 250100, PR China b Department of Chemistry and Chemical Engineering, Qilu Normal University, Shandong Province, 36# Lishan Road, Jinan 250013, PR China c Shandong Supervision and Inspection Institute for Product Quality, Shandong Province, 81# Shanda North Road, Jinan 250100, PR China d America CRC for Environment & Health, Shandong Province, 27# Shanda South Road, Jinan 250100, PR China |
| Abstract: | The interaction of La3+ to bovine serum albumin (BSA) has been investigated mainly by fluorescence spectra, UV-vis absorption spectra, and circular dichroism (CD) under simulative physiological conditions. Fluorescence data revealed that the quenching mechanism of BSA by La3+ was a static quenching process and the binding constant is 1.75×104 L mol−1 and the number of binding sites is 1 at 289 K. The thermodynamic parameters (ΔH=−20.055 kJ mol−1, ΔG=−23.474 kJ mol−1, and ΔS=11.831 J mol−1 K−1) indicate that electrostatic effect between the protein and the La3+ is the main binding force. In addition, UV-vis, CD, and synchronous fluorescence results showed that the addition of La3+ changed the conformation of BSA. |
| Keywords: | Lanthanum Bovine serum albumin Fluorescence spectra UV-vis absorption spectra |
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