Probing the interaction between levamlodipine and hemoglobin based on spectroscopic and molecular docking methods

Xu, Linlin; Liu, Zhao‐Qing; Liao, Tancong; Tuo, Xun

doi:10.1016/j.saa.2019.117306

Cited by 16 publications

(6 citation statements)

References 39 publications

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“…The endogenous fluorescence of the protein is mainly derived from the two aromatic amino acid residues, Tyr and Trp, where Tyr exists in the two binding sites and Trp only exists in site I. Hence, the difference in fluorescence characteristics between Trp and Tyr was studied and used to explore the binding site between SMT and HSA [ 32 ]. The influence of SMT on HSA fluorescence intensity was tested at different excitation wavelengths (280 nm and 295 nm).…”

Section: Resultsmentioning

confidence: 99%

Interactions between Human Serum Albumin and Sulfadimethoxine Determined Using Spectroscopy and Molecular Docking

Zhang

Cao

et al. 2022

Molecules

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Sulfonamides are widely used antibiotics in agricultural production. However, the potential threat of these drugs to human health has increased global concern. Human serum albumin (HSA) is the main reservoir and transporter of exogenous small molecules in humans. In this study, the interaction between sulfadimethoxine (SMT) and human serum albumin (HSA) was studied using spectroscopy and computer simulation. Our results showed that the hydrogen bonding and van der Waals forces drove SMT to enter the binding site I of HSA spontaneously and resulted in the fluorescence quenching of HSA. The stability of the HSA–SMT complex decreased with an increase in temperature. The binding of SMT to HSA induced alterations in the secondary structure of HSA, where the content of α-helix decreased from 61.0% of the free state to 59.0% of the compound state. The π–π, π–σ, and π–alkyl interactions between HSA and SMT were found to play important roles in maintaining the stability of the complex.

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Section: Resultsmentioning

confidence: 99%

Interactions between Human Serum Albumin and Sulfadimethoxine Determined Using Spectroscopy and Molecular Docking

Zhang

Cao

et al. 2022

Molecules

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“…The main advantage over using slaughterhouse blood compared to outdated human blood in research is the fact that slaughterhouse blood is abundant, while a maximum of 5-10% donated human blood is not used for transfusion (becomes outdated [5] or contains anti-erythrocyte antibodies) and can be used for biotechnological purposes. Thus far, hemoglobin isolated from slaughterhouse blood has found application in studies of the interactions of proteins with ligands, molecules, and nanoparticles, and their harmfulness and safety [28][29][30][31], as a biosensor and drug carrier [29], and, to the greatest extent, as hemoglobin-based oxygen carriers [1,3]. Porcine Hb (PHb) has also been added to the portfolio of raw materials for this type of oxygen carrier [32], as a result of the restricted stock of human Hb and the potential danger of human blood-borne diseases such as hepatitis and HIV and cross-species transmission of Creutzfeldt-Jakob disease (mad cow disease) in the case of bovine blood use.…”

Section: Discussionmentioning

confidence: 99%

Modulation of Functional Characteristics of Mesenchymal Stromal Cells by Acellular Preparation of Porcine Hemoglobin

et al. 2021

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Exploring the potential usage of the acellular preparation of porcine hemoglobin (PHb) isolated from slaughterhouse blood as a cell culture media component, we have tested its effects on the functional characteristics of stromal cells of mesodermal origin. Human peripheral blood mesenchymal stromal cells (PB-MSCs) were used in this study as a primary cell model system, along with three mouse cell lines (ATDC5, MC3T3-E1, and 3T3-L1), which represent more uniform model systems. We investigated the effect of PHb at concentrations of 0.1, 1, and 10 μM on these cells’ proliferation, cycle, and clonogenic and migratory potential, and found that PHb’s effect depended on both the cell type and its concentration. At the lowest concentration used (0.1 μM), PHb showed the least evident impact on the cell growth and migration; hence, we analyzed its effect on mesenchymal cell multilineage differentiation capacity at this concentration. Even under conditions that induce a specific type of MSC differentiation (cultivation in particular differentiation media), PHb modulated chondrogenic, osteogenic, and adipogenic differentiation, making it a potential candidate for a supplement of MSC culture. Through a model of porcine hemoglobin, these findings also contribute to improving the knowledge of extracellular hemoglobin’s influence on MSCs >in vivo.

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“…Fluorescence spectroscopy has been an effective method for the study of the interactions between small molecules and proteins 51 . TY has strong intrinsic fluorescence near 346 nm.…”

Section: Resultsmentioning

confidence: 99%

“…Fluorescence spectroscopy has been an effective method for the study of the interactions between small molecules and proteins. 51 TY has strong intrinsic fluorescence near 346 nm. The interaction between TY and DG was investigated by the fluorescence spectra at wavelengths of 300-500 nm upon excitation at 280 nm.…”

Section: Fluorescence Quenching Mechanism Of Ty By Dgmentioning

confidence: 99%

Spectroscopic studies and molecular docking on the interaction of delphinidin‐3‐O‐galactoside with tyrosinase

Chen

Shi

Liu

et al. 2021

Biotech and App Biochem

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The inhibitory effects of delphinidin-3-O-galactoside (DG) on the activities of tyrosinase (EC 1.14.18.1) (TY) from the edible Agaricus bisporus mushroom were investigated by enzyme kinetics, multispectroscopic methods, and molecular docking. As a result, DG showed strong inhibition on TY with the IC 50 of 34.14 × 10 -6 mol L -1 . The inhibition mode of DG against TY was mixed type with α values of 5.09. The binding constant K a and related thermodynamic parameters at the three different temperatures showed that the fluorescence quenching of TY by DG was static quenching. Synchronous fluorescence, three-dimensional fluorescence, ultraviolet-visible spectroscopy, and circular dichroism spectroscopies confirmed that the conformation or microenvironment of the TY protein were changed after binding with DG. Molecular docking revealed that DG had strong binding affinity to TY through hydrogen bonding and van der Waals force, and the results were consistent with the fluorescence data. Our findings suggested that DG may be potential TY inhibitor.

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Probing the interaction between levamlodipine and hemoglobin based on spectroscopic and molecular docking methods

Cited by 16 publications

References 39 publications

Interactions between Human Serum Albumin and Sulfadimethoxine Determined Using Spectroscopy and Molecular Docking

Interactions between Human Serum Albumin and Sulfadimethoxine Determined Using Spectroscopy and Molecular Docking

Modulation of Functional Characteristics of Mesenchymal Stromal Cells by Acellular Preparation of Porcine Hemoglobin

Spectroscopic studies and molecular docking on the interaction of delphinidin‐3‐O‐galactoside with tyrosinase

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