In vitro and in silico Determination of the Interaction of Artemisinin with Human Serum Albumin

2020 ◽  
Vol 54 (4) ◽  
pp. 586-598
Author(s):  
S. Ginosyan ◽  
H. Grabski ◽  
S. Tiratsuyan
Keyword(s):  
Human Serum Albumin ◽  
Serum Albumin ◽  
Human Serum ◽  
In Silico

Nof2206Probing the interaction of memantine, an important Alzheimer's drug, with human serum albumin: In silico and In vitro approach

2021 ◽  
pp. 116888
Author(s):  
Fahad A. Alhumaydhi ◽  
Mohammad Abdullah Aljasir ◽  
Abdullah S.M. Aljohani ◽  
Suliman A. Alsagaby ◽  
Ameen S.S. Alwashmi ◽  
...  
Keyword(s):  
Human Serum Albumin ◽  
Serum Albumin ◽  
Human Serum ◽  
In Silico

Molecular mechanism of tobramycin with human serum albumin for probing binding interactions: multi-spectroscopic and computational approaches

2017 ◽  
Vol 41 (16) ◽  
pp. 8203-8213 ◽  
Author(s):  
Muslim Raza ◽  
Yun Wei ◽  
Yang Jiang ◽  
Aftab Ahmad ◽  
Saleem Raza ◽  
...  
Keyword(s):  
Human Serum Albumin ◽  
Serum Albumin ◽  
Human Serum ◽  
Binding Site ◽  
Molecular Mechanism ◽  
In Silico ◽  
The Novel ◽  
Binding Interactions ◽  
Computational Approaches

Highlighting novelty: comprehensive in vitro and in silico insights for understanding the novel binding site of TOB with HSA.

Synthesis, characterization, in vitro cytotoxicity, in silico ADMET analysis and interaction studies of 5-dithiocarbamato-1,3,4-thiadiazole-2-thiol and its zinc(ii) complex with human serum albumin: combined spectroscopy and molecular docking investigations

RSC Advances ◽  
2016 ◽  
Vol 6 (108) ◽  
pp. 106516-106526 ◽  
Author(s):  
Fereshteh Shiri ◽  
Somaye Shahraki ◽  
Sadegh Baneshi ◽  
Massoud Nejati-Yazdinejad ◽  
Mostafa Heidari Majd
Keyword(s):  
Molecular Docking ◽  
Human Serum Albumin ◽  
Serum Albumin ◽  
Human Serum ◽  
Binding Site ◽  
In Silico ◽  
In Vitro Cytotoxicity ◽  
Interaction Studies ◽  
In Silico Admet

The binding site of new complex Zn(ii) of 5-dithiocarbamato-1,3,4-thiadiazole-2-thiol and HAS.

scholarly journals Are Zinc oxide nanoparticles safe? A structural study on human serum albumin using in vitro and in silico methods

2018 ◽  
Author(s):  
Marziyeh Hassanian ◽  
Hassan Aryapour ◽  
Alireza Goudarzi ◽  
Masoud Bezi Javan
Keyword(s):  
Zinc Oxide ◽  
Human Serum Albumin ◽  
Serum Albumin ◽  
Human Serum ◽  
In Silico ◽  
Zinc Oxide Nanoparticles ◽  
Protein Corona ◽  
Oxide Nanoparticles ◽  
Zno Nps

AbstractWith due attention to adsorption of proteins on the nanoparticles surface and the formation of nanoparticle-protein corona, investigation of nanoparticles toxicity on the structure of proteins is important. Therefore, this work was done to evaluate toxicity of Zinc oxide nanoparticles (ZnO NPs) on the structure of human serum albumin (HSA) through in vitro and in silico studies. First, ZnO NPs were synthesized using hydrothermal method and their size and morphology were determined by SEM and TEM methods and then to study its toxicity on the HSA structure were used UV-Vis and fluorescence spectroscopy. Also, in order to investigate interaction mechanism of ZnO NP with HSA at the atomistic level was used molecular dynamics (md) simulation. The obtained images from SEM and TEM showed that ZnO NPs were nanosheet with size of less than 40 nm. The results of spectroscopic studies showed ZnO NPs lead to significant conformational changes in the protein’s absorption and emission spectra. Moreover, md results showed the minor structure changes in HSA due to interaction with ZnO NP during the 100 ns simulation and the formation of nanoparticle-protein corona complex that is mainly because of electrostatic interactions between charge groups of HSA and ZnO NP.

scholarly journals Effects of human serum albumin on post-mortem changes of malathion

2021 ◽  
Vol 11 (1) ◽  
Author(s):  
Yoshikazu Yamagishi ◽  
Hirotaro Iwase ◽  
Yasumitsu Ogra
Keyword(s):  
Human Serum Albumin ◽  
Serum Albumin ◽  
Human Serum ◽  
Lethal Dose ◽  
Free Form ◽  
Post Mortem ◽  
Flight Mass Spectrometry ◽  
Dose Dependent Fashion

AbstractMalathion, diethyl 2-[(dimethoxyphosphinothioyl)thio]butanedioate, is one of most widely used organophosphoryl pesticide, and it has been detected in several clinical cases of accidental exposure and suicide. It is reported that the observed malathion concentration in blood of persons who suffer from malathion poisoning is smaller than the expected concentration. Because malathion is bound to human serum albumin (HSA), recovery of malathion in the free form is insufficient. We detected malathion adducts in HSA by liquid chromatography quadrupole time-of-flight mass spectrometry (LC-Q/TOF–MS). The mass spectra showed that malathion was preferably bound to the lysine (K) and cysteinylproline (CP) residues of HSA. The K- and CP-adducts of malathion were increased in vitro with a dose-dependent fashion when its concentration was smaller than the lethal dose. Further, the K-adduct was also detected in post-mortem blood of an autopsied subject suffering from intentional malathion ingestion. These results suggest that the K-adduct seems to be available to use a biomarker of malathion poisoning, and the determination of the K-adduct could make possible to estimate the amount of malathion ingestion.

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