scholarly journals Human serum albumin immobilization on APTES coated magnetite nanoparticles

2014 ◽  
Vol 17 (3) ◽  
pp. 41-51
Author(s):  
Thanh Trung Bui ◽  
Van Hung Pham ◽  
Hai Hoang Tran
Keyword(s):  
Human Serum Albumin ◽  
Serum Albumin ◽  
Human Serum ◽  
Magnetite Nanoparticles ◽  
Gravimetric Analysis ◽  
Vibrating Sample Magnetometer ◽  
Thermal Gravimetric ◽  
Transmission Electron ◽  
Vis Spectroscopy ◽  
Co Precipitation

Magnetite nanoparticles were synthesized by co-precipitation of Fe2+ and Fe3+ with NH3.H20, and then 3- aminopropyltriethoxysilane (APTES) was coated on the magnetite nanoparticles by silanization reaction to achieve Fe3O4/APTES nanostructures. After modified by APTES, the nanostructures were activated by glutaraldehyde (GA) to obtain functional groups on the nanostructures surface. Human Serum Albumin (HSA) was immobilised on the Fe3O4/APTES and Fe3O4/APTES/GA nanostructures. The morphology and properties of the nanoparticles were characterized by transmission electron microscopy (TEM), Xray diffraction (XRD), vibrating sample magnetometer (VSM), Fourier transform infrared spectroscopy (FTIR), UV–vis spectroscopy and thermal gravimetric analysis (TGA). The HSA binding efficiency was estimated by the Bradford method.

Characterization of the interaction between human serum albumin and diazinon via spectroscopic and molecular docking methods

2018 ◽  
Vol 37 (9) ◽  
pp. 959-971
Author(s):  
S Hadichegeni ◽  
B Goliaei ◽  
M Taghizadeh ◽  
S Davoodmanesh ◽  
F Taghavi ◽  
...  
Keyword(s):  
Molecular Docking ◽  
Human Serum Albumin ◽  
Serum Albumin ◽  
Human Serum ◽  
Blood Protein ◽  
Vis Spectroscopy ◽  
Close Relationship ◽  
Partially Unfolded ◽  
Α Helix ◽  
Toxic Concentrations

Human serum albumin (HSA) is a soluble blood protein which binds to small molecules (such as drugs and toxins) and transfers them within the blood circulation. In this research, the interaction of diazinon, as a toxic organophosphate, with HSA was investigated. Various biophysical methods such as fluorescence, ultraviolet–visible (UV-vis), Fourier transform infrared spectroscopy, and molecular docking were utilized to characterize the binding properties of diazinon to HSA under physiological-like condition. The UV-vis spectroscopy showed that the absorption increased and the fluorescence intensity of HSA decreased regularly with regard to the gradual increases of the concentrations of diazinon. Due to the binding constant of ( ka = 3.367 × 10+4 M−1), the α-helix structure for the first day and 35 days of incubation were obtained 66.09–55.4% and 59.99–46.48%, respectively, and their amounts in other secondary structures (β-sheet, β-anti, and random (r) coils) were increased. The molecular docking revealed a good binding site in HSA (Trp-214) for diazinon which was related to the considerable alterations in HSA secondary and tertiary structures. There is a close relationship between the secondary structure of protein and its biological activity and after 35 days of incubation, the high toxic concentrations of diazinon can make HSA to be partially unfolded and lose its structure.

scholarly journals Molecular Basis of Interactions between the Antibiotic Nitrofurantoin and Human Serum Albumin: A Mechanism for the Rapid Drug Blood Transportation

2021 ◽  
Vol 22 (16) ◽  
pp. 8740
Author(s):  
Antonella Calderaro ◽  
Alessandro Maugeri ◽  
Salvatore Magazù ◽  
Giuseppina Laganà ◽  
Michele Navarra ◽  
...  
Keyword(s):  
Human Serum Albumin ◽  
Serum Albumin ◽  
Human Serum ◽  
Binding Site ◽  
Biological Effects ◽  
Protein Secondary Structure ◽  
Ligand Docking ◽  
Fluorescence Studies ◽  
Biological Potential ◽  
Vis Spectroscopy

Nitrofurantoin is an antimicrobial agent obtained through the addition of a nitro group and a side chain containing hydantoin to a furan ring. The interactions of the antibiotic with human serum albumin (HSA) have been investigated by fluorescence, UV-VIS, Fourier transform infrared spectroscopy (FTIR) spectroscopy, and protein-ligand docking studies. The fluorescence studies indicate that the binding site of the additive involves modifications of the environment around Trp214 at the level of subdomain IIA. Fluorescence and UV-VIS spectroscopy, displacement studies, and FTIR experiments show the association mode of nitrofurantoin to HSA, suggesting that the primary binding site of the antibiotic is located in Sudlow’s site I. Molecular modeling suggests that nitrofurantoin is involved in the formation of hydrogen bonds with Trp214, Arg218, and Ser454, and is located in the hydrophobic cavity of subdomain IIA. Moreover, the curve-fitting results of the infrared Amide I’ band indicate that the binding of nitrofurantoin induces little change in the protein secondary structure. Overall, these data clarify the blood transportation process of nitrofurantoin and its rapid transfer to the kidney for its elimination, hence leading to a better understanding of its biological effects and being able to design other molecules, based on nitrofurantoin, with a higher biological potential.

scholarly journals Interaction of Mitoxantrone-Loaded Cholesterol Modified Pullulan Nanoparticles with Human Serum Albumin and Effect on Drug Release

2019 ◽  
Vol 2019 ◽  
pp. 1-13 ◽  
Author(s):  
Liming Yuan ◽  
Bu Guo ◽  
Wu Zhong ◽  
Yu Nie ◽  
Xiaoyan Yao ◽  
...  
Keyword(s):  
Human Serum Albumin ◽  
Drug Release ◽  
Serum Albumin ◽  
Human Serum ◽  
Electrostatic Force ◽  
Spherical Shape ◽  
Interaction Force ◽  
Titration Calorimetry ◽  
Size Change ◽  
Transmission Electron

To clarify nanoparticle-protein interaction and their action characteristics, the interactions between MTO-CHP NPs and human serum albumin (HSA) were studied by isothermal titration calorimetry (ITC), fluorescence spectroscopy, dynamic light scattering (DLS), and circular dichroism spectroscopy (CD). Hydrophobically modified pullulan (CHP) nanoparticles (NPs) loaded with mitoxantrone (MTO) were prepared (MTO-CHP NPs) with size 166.9 nm. The spherical shape was verified by transmission electron microscopy (TEM). The ITC results demonstrated an interaction between MTO-CHP NPs mainly by hydrophobic interaction force, electrostatic force, and hydrogen bonding. The mean binding constant KA was 0.832×104 M−1 and mean HSA coverage 0.939±0.302. MTO-CHP NPs could quench the fluorescence intensity of HSA, which gradually decreased to be balanced in 9 h and indicated the completion of the complexation. The size and zeta potential changes of the combined particle were dynamically detected with DLS at 0, 3, 6, 9, 12, 15, and 18 h. When the reaction was completed at 9 h, the particle size and potential remained stable, accompanied by a size change from 89.91 to about 145 nm and potential change from -15 to -3 mV, respectively. The results of CD measurement showed that the change in ellipticity of HSA at 208 nm was similar to the fluorescence spectra and DLS measurements with MTO-CHP NPs combined with HSA. At the beginning of the reaction, the proportion of α-helix was 52.3% to 43.7%, which decreased by 39.1% at compound stabilization. The release of MTO from MTO-CHP NPs at pH=5.6 was significantly accelerated, whereas that of MTO from HSA-MTO-CHP NPs was significantly reduced, and the drug release was significantly slowed down even under acidic conditions, which indicates the beneficial effect of HSA on the persistence and stability of the HSA-MTO-CHP NP compound.

scholarly journals Bioactive anthraquinones found in plant foods interact with human serum albumin and inhibit the formation of advanced glycation endproducts

2018 ◽  
Vol 4 ◽  
Author(s):  
Weixi Liu ◽  
Ang Cai ◽  
Rachel Carley ◽  
Robert Rocchio ◽  
Zoe M. Petrovas ◽  
...  
Keyword(s):  
Protein Structure ◽  
Human Serum Albumin ◽  
Serum Albumin ◽  
Human Serum ◽  
Advanced Glycation Endproducts ◽  
Critical Role ◽  
Titration Calorimetry ◽  
Vis Spectroscopy ◽  
Anthraquinone Derivatives ◽  
Aloe Emodin

The glycation of human serum albumin (HSA) plays a critical role in the development of many disorders. Herein, the anti-glycation effects of several natural dietary anthraquinone derivatives including aloin, aloe-emodin, chrysophanol, emodin, physcion, and rhein were evaluated. The anthraquinones at 100 μM reduced fructose-, methylglyoxal-, and glyoxal-induced HSA glycation by 21% (aloe-emodin) to 92% (aloin), 17% (physcion) to 94% (emodin), and 16% (anthraquinone) to 67% (emodin), respectively. These anthraquinone derivatives also protected HSA by maintaining its free amino acid residues and secondary protein structure as characterized by circular dichroism. The mechanisms of their anti-glycation effects were investigated using rhein as a representative anthraquinone. The interactions between rhein and HSA were evaluated by biophysical characterizations, namely, isothermal titration calorimetry and UV-vis spectroscopy as well as computational modeling. Our findings suggest that the anti-glycation effects of these anthraquinones may be attributed to their binding capacity and stabilization of the HSA protein structure.

Preparation and radiolabeling of human serum albumin (HSA)-coated magnetite nanoparticles for magnetically targeted therapy

2004 ◽  
Vol 61 (6) ◽  
pp. 1255-1259 ◽  
Author(s):  
Zhang Chunfu ◽  
Cao Jinquan ◽  
Yin Duanzhi ◽  
Wang Yongxian ◽  
Feng Yanlin ◽  
...  
Keyword(s):  
Targeted Therapy ◽  
Human Serum Albumin ◽  
Serum Albumin ◽  
Human Serum ◽  
Magnetite Nanoparticles

Effect of Fe3+ on the Interaction between Nitrofurazone and Human Serum Albumin by Spectroscopic Analysis

2012 ◽  
Vol 518-523 ◽  
pp. 337-340
Author(s):  
Feng Yu Deng ◽  
Ying Liu
Keyword(s):  
Human Serum Albumin ◽  
Serum Albumin ◽  
Human Serum ◽  
Metal Ion ◽  
Fluorescence Spectra ◽  
Storage Time ◽  
Spectroscopic Analysis ◽  
Effect Model ◽  
Vis Spectroscopy ◽  
Binding Distance

The effect of Fe3+ on the interaction between nitrofurazone (NF) and human serum albumin (HSA) was studied by fluorescence spectroscopy and UV-vis spectroscopy. The results from fluorescence spectra showed that Fe3+ increased the binding constant of NF to HSA, indicating longer storage time of NF in blood plasma. The effect model of Fe3+ was researched by binding distance and the UV-vis spectra, which showed that in the HSA-NF-Fe ternary system Fe-NF complex formed via metal ion bridge and enhanced the binding capability of NF to HSA.

Novel nanochemistry toward generation and stabilization of gold nanoparticles in human serum albumin matrix

2011 ◽  
Vol 83 (11) ◽  
pp. 2055-2062 ◽  
Author(s):  
Raghuraman Kannan ◽  
Satish Nune ◽  
Nripen Chanda ◽  
Ajit Zambre ◽  
Ravi Shukla
Keyword(s):  
Gold Nanoparticles ◽  
Human Serum Albumin ◽  
Serum Albumin ◽  
Human Serum ◽  
Evaluation Studies ◽  
Toxicity Evaluation ◽  
Cellular Toxicity ◽  
The Core ◽  
Transmission Electron

The interactions of gold nanoparticles (AuNPs) with human serum albumin (HSA) greatly influence their in vivo characteristics. It is important to develop conjugates that can serve as ideal structural models to understand the interaction of AuNPs with HSA. We report the synthesis and stabilization of AuNPs in HSA matrix with no additional ligands on the surface of the NPs. The hydrodynamic size of the AuNP–HSA conjugate is 22 nm, and transmission electron microscopy (TEM) measurement shows the core size as 8–13 nm. We have performed strip assay to establish that the biological activity of HSA is retained even after conjugation. Our cellular toxicity evaluation studies show that AuNP–HSA conjugates are nontoxic and biocompatible.

II. Lokalisation der Placenta mit 113Inm- Human-Serum-Albumin

1969 ◽  
Vol 08 (01) ◽  
pp. 15-21 ◽  
Author(s):  
K. E. Scheer ◽  
J. Heep ◽  
W. Maier-Borst ◽  
W. J. Lorenz ◽  
H. Sinn ◽  
...  
Keyword(s):  
Human Serum Albumin ◽  
Serum Albumin ◽  
Human Serum ◽  
Vena Cava ◽  
Placenta Praevia ◽  
Wird Eine

ZusammenfassungNach tierexperimentellen Voruntersuchungen wurde die Placentographie mit trägerfreiem 113Inm -HSA als klinische Methode eingeführt. Vor Amniocentesen und bei Verdacht auf Placenta praevia werden Placentographien geschrieben. Den Schwangeren wird eine Aktivität von 500 μCi in die Cubitalvene injiziert. Die der Aktivität entsprechende Indiummenge ist kleiner als 0,1 ng. Die fetale Strahlenbelastung liegt unter lOmrad. Bei Anwendung von 113Inm-HSA entfällt eine Blockade der mütterlichen und fetalen Schilddrüsen. Die genaue Abgrenzung einer Placenta praevia wird nicht durch eine Blasenaktivität beeinträchtigt.Es wurden bisher 19 Placentalokalisationen durchgeführt. In allen Fällen konnte der Placentasitz eindeutig festgestellt werden. Bedingt durch die lange Liegezeit beim Aufnehmen eines Szintigramms kam es in zwei Fällen zu einem Vena-Cava-Kompressions-Syndrom. Zur Verhinderung dieser klinischen Zwischenfälle werden inzwischen Placentographien mit der Anger-Kamera aufgenommen. Mit Hilfe des divergierenden Kollimators konnte der gesamte Abdominalbereich erfaßt werden. Die Aufnahmezeit konnte auf 7 — 10 Minuten verkürzt werden. Die intravenöse injizierte Aktivität betrug bei dieser Methode ebenfalls 500 μCi. Der diagnostische Aussagewert der Kamerabilder ist szintigraphischen Aufnahmen gleichwertig.

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