Study of interaction between syringin and human serum albumin by multi-spectroscopic method and atomic force microscopy

Gao, Wenhua; Li, Nana; Chen, Yaowen; Xu, Yanping; Lin, Yuejuan; Yin, Yuan‐Qi; Hu, Zhide

doi:10.1016/j.molstruc.2010.08.042

Cited by 35 publications

(14 citation statements)

References 35 publications

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“…It can be seen from Figure that there was no fluorescence emission for MON at the range measured; however, fluorescence intensity of HSA decreased gradually upon increase of MON concentration along with a remarkable blue shift of the emission maximum. These results indicate that HSA interacted with MON and the chromophore of tryptophan in HSA was placed in a more hydrophobic environment after the addition of MON . The Stern–Volmer equation was used to analyze fluorescence quenching of HSA initiated by MON as per Equation ():

F_{0} / F = 1 + K SV [Q] = 1 + K q τ_{0} [Q]

where F 0 and F denote fluorescence intensities in the absence and presence of quencher (MON), respectively.…”

Section: Resultsmentioning

confidence: 99%

4‐alkoxyethoxy‐N‐octadecyl‐1,8‐naphthalimide fluorescent sensor for human serum albumin and other major blood proteins: design, synthesis and solvent effect

et al. 2012

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A series of 4-alkoxyethoxy-N-octadecyl-1,8-naphthalimides with intense blue fluorescence were designed and synthesized as polarity and spectrofluorimetric probes for the determination of proteins. In solvents of different polarities, the Stokes shifts of two dyes increased with increasing solvent polarity and fluorescence quantum yields decreased significantly, suggesting that electronic transiting from ground to excited states was π-π(*) in character. Dipole moment changes were estimated from solvent-dependent Stokes shift data using a solvatochromic method based on bulk solvent polarity functions and the microscopic solvent polarity parameter (E(T)N). These results were generally consistent with semi-empirical molecular orbital calculations and were found to be quite reliable based on the fact that the correlation of the solvatochromic Stokes shifts with E(T)N was superior to that obtained using bulk solvent polarity functions. Fluorescence data revealed that the fluorescence quenching of human serum albumin (HSA) by dyes was the result of the formation of a Dye-HSA complex. The method was applied to the determination of total proteins (HSA + immunoglobulins) in human serum samples and results were in good agreement with those reported by the research institute.

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F_{0} / F = 1 + K SV [Q] = 1 + K q τ_{0} [Q]

where F 0 and F denote fluorescence intensities in the absence and presence of quencher (MON), respectively.…”

Section: Resultsmentioning

confidence: 99%

4‐alkoxyethoxy‐N‐octadecyl‐1,8‐naphthalimide fluorescent sensor for human serum albumin and other major blood proteins: design, synthesis and solvent effect

et al. 2012

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“…e results signified that the binding site of SBAL was near the Trp214 in HSA and the Trp214 microenvironment was altered to more hydrophobic [21]. e effect of SBAL on the fluorescence intensity of HSA is similar to the interaction between syringin and HSA [20].…”

Section: Effect Of Sbal On the Intrinsic Fluorescence Of Hsamentioning

confidence: 89%

“…But the quantum yield of Phe residue is very low, and the fluorescence intensity of Tyr residue is almost completely quenched when it is ionized or close to an amino group, a carboxyl group, or a Trp. So, the intrinsic fluorescence of HSA mainly comes from only one Trp214 [20]. e Trp214 is located in subdomain IIA of Sudlow's binding site I and gave the strongest emission at about 340 nm in the fluorescence spectrum of HSA when the excitation wavelength is 295 nm.…”

Section: Effect Of Sbal On the Intrinsic Fluorescence Of Hsamentioning

confidence: 96%

Investigation of the Interaction Mechanism between Salbutamol and Human Serum Albumin by Multispectroscopic and Molecular Docking

Zhao

Liu

Niu

et al. 2020

BioMed Research International

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Salbutamol (SBAL), a kind of short-acting beta 2-adrenergic agonist, has been mainly used to treat bronchial asthma and other allergic airway diseases clinically. In this study, the interaction mechanism between salbutamol and human serum albumin was researched by the multispectral method and molecular docking. The fluorescence intensity of HSA could be regularly enhanced with the increase of SBAL concentration. Both the results of the multispectral method and molecular docking showed that SBAL could bind HSA with van der Waals force and hydrogen bonds. The binding mechanism was further analysed by UV-Vis and synchronous fluorescence spectra. The contents of the secondary structure of free HSA and SBAL-HSA complex were evaluated using CD spectra.

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“…However, the intensity of BSA intrinsic fluorescence increased with the increasing Syr concentration. In this condition, the fluorescence data were analyzed by the Lineweaver-Burk equation as follows [40,41], and the result was shown in Fig 7.…”

Section: Fluorescence Parameter Analysismentioning

confidence: 99%

“…Previous studies demonstrated that salvianolic acids from Danshen (Radix Salviae Miltiorrhizae), and nucleosides, flavonoids, phenylethanoid glycosides from Honghua (Flos Carthami Tinctorii) might be the most potent active components for the therapeutic effect of DHI [12][13][14][15]. In vitro experiments have identified some of these natural components binding to HSA or BSA [16][17][18][19],but many components still need to be carefully studied. These studies were carried out under relatively "pure" conditions, ignoring the complex conditions under which natural products exist in plants.…”

Section: Introductionmentioning

confidence: 99%

Interaction between the Natural Components in Danhong Injection (DHI) with Serum Albumin (SA) and the Influence of the Coexisting Multi-Components on the SaB-BSA Binding System: Fluorescence and Molecular Docking Studies

et al. 2015

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Danhong injection (DHI) is a widely used Chinese Materia Medica standardized product for the clinical treatment of ischemic encephalopathy and coronary heart disease. The bindings of eight natural components in DHI between bovine serum albumin (BSA) were studied by fluorescence spectroscopy technology and molecular docking. According to the results, the quenching process of salvianolic acid B and hydroxysafflor yellow A was a static quenching procedure through the analysis of quenching data by the Stern-Volmer equation, the modified Stern-Volmer equation, and the modified Scatchard equation. Meanwhile, syringin (Syr) enhanced the fluorescence of BSA, and the data were analyzed using the Lineweaver-Burk equation. Molecular docking suggested that all of these natural components bind to serum albumin at the site I location. Further competitive experiments of SaB confirmed the result of molecular docking studies duo to the displacement of warfarin by SaB. Base on these studies, we selected SaB as a research target because it presented the strongest binding ability to BSA and investigated the influence of the multi-components coexisting in DHI on the interaction between the components of the SaB-BSA binding system. The participation of these natural components in DHI affected the interaction between the components of the SaB-BSA system. Therefore, when DHI is used in mammals, SaB is released from serum albumin more quickly than it is used alone. This work would provide a new experiment basis for revealing the scientific principle of compatibility for Traditional Chinese Medicine.

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Study of interaction between syringin and human serum albumin by multi-spectroscopic method and atomic force microscopy

Cited by 35 publications

References 35 publications

4‐alkoxyethoxy‐N‐octadecyl‐1,8‐naphthalimide fluorescent sensor for human serum albumin and other major blood proteins: design, synthesis and solvent effect

4‐alkoxyethoxy‐N‐octadecyl‐1,8‐naphthalimide fluorescent sensor for human serum albumin and other major blood proteins: design, synthesis and solvent effect

Investigation of the Interaction Mechanism between Salbutamol and Human Serum Albumin by Multispectroscopic and Molecular Docking

Interaction between the Natural Components in Danhong Injection (DHI) with Serum Albumin (SA) and the Influence of the Coexisting Multi-Components on the SaB-BSA Binding System: Fluorescence and Molecular Docking Studies

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