Abstract
Background: Nicotine is the main tobacco alkaloid that leads to smoking addiction. Human serum albumin (HSA) is the most abundant protein present in the circulatory system. Nuclear magnetic resonance (NMR) has been widely used for studying the interactions of small molecules with macromolecules. The proton spin relaxation rate of the small molecule has proved to be a suitable parameter in ligand– macromolecule complex studies.
Objective: In-depth study nicotine interact with HSA.
Method: Spin-lattice relaxation, molecular modeling, fluorescence, FT-IR and CD spectrometers were chosen for this study.
Results: HSA caused a change in the H-4 and H-9 of a nicotine proton environment. The values of normalized affinity index for the H-4/H-9 proton were (7996.9 ± 374.4) and (6840.8 ± 351.6) L·mol-1, respectively. Nicotine showed a good fit with Sudlow site II, and hydrogen bonds performed a significant function in the nicotine–HSA interaction. Citric acid exerted a slight effect, whereas malic acid exhibited an evident effect on the interaction. FT-IR and CD results revealed that nicotine–HSA interaction slightly affected the secondary structure of HSA.
Conclusion: Nicotine can effectively combine with HSA and influence the native structure of HSA.
Keywords: Human serum albumin, molecular modeling, nicotine, nuclear magnetic resonance, spin relaxation, structure change.
Current Analytical Chemistry
Title:A New Perspective on Probing the Interaction of Nicotine with Human Serum Albumin
Volume: 12 Issue: 5
Author(s): Xiaoxiang Liao, Jianguo Tang, Jiawei He, Dalin Yuan, Bing Liang, Qiang Cheng and Hui Li
Affiliation:
Keywords: Human serum albumin, molecular modeling, nicotine, nuclear magnetic resonance, spin relaxation, structure change.
Abstract: Background: Nicotine is the main tobacco alkaloid that leads to smoking addiction. Human serum albumin (HSA) is the most abundant protein present in the circulatory system. Nuclear magnetic resonance (NMR) has been widely used for studying the interactions of small molecules with macromolecules. The proton spin relaxation rate of the small molecule has proved to be a suitable parameter in ligand– macromolecule complex studies.
Objective: In-depth study nicotine interact with HSA.
Method: Spin-lattice relaxation, molecular modeling, fluorescence, FT-IR and CD spectrometers were chosen for this study.
Results: HSA caused a change in the H-4 and H-9 of a nicotine proton environment. The values of normalized affinity index for the H-4/H-9 proton were (7996.9 ± 374.4) and (6840.8 ± 351.6) L·mol-1, respectively. Nicotine showed a good fit with Sudlow site II, and hydrogen bonds performed a significant function in the nicotine–HSA interaction. Citric acid exerted a slight effect, whereas malic acid exhibited an evident effect on the interaction. FT-IR and CD results revealed that nicotine–HSA interaction slightly affected the secondary structure of HSA.
Conclusion: Nicotine can effectively combine with HSA and influence the native structure of HSA.
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Cite this article as:
Liao Xiaoxiang, Tang Jianguo, He Jiawei, Yuan Dalin, Liang Bing, Cheng Qiang and Li Hui, A New Perspective on Probing the Interaction of Nicotine with Human Serum Albumin, Current Analytical Chemistry 2016; 12 (5) . https://dx.doi.org/10.2174/1573411012999160721160103
DOI https://dx.doi.org/10.2174/1573411012999160721160103 |
Print ISSN 1573-4110 |
Publisher Name Bentham Science Publisher |
Online ISSN 1875-6727 |
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