scholarly journals Fabrication and Characterization of Human Serum Albumin Particles Loaded with Non-Sericin Extract Obtained from Silk Cocoon as a Carrier System for Hydrophobic Substances

Polymers ◽  
2021 ◽  
Vol 13 (3) ◽  
pp. 334
Author(s):  
Kanyaluck Jantakee ◽  
Ausanai Prapan ◽  
Saranya Chaiwaree ◽  
Nittiya Suwannasom ◽  
Waraporn Kaewprayoon ◽  
...  
Keyword(s):  
Human Serum Albumin ◽  
Serum Albumin ◽  
Human Serum ◽  
Biological Effects ◽  
Ethanolic Extract ◽  
Aqueous Solubility ◽  
Carrier System ◽  
Hydrophobic Substances ◽  
Particle Localization ◽  
Lung Adenocarcinoma A549

Non-sericin (NS) extract was produced from the ethanolic extract of Bombyx mori silk cocoons. This extract is composed of both carotenoids and flavonoids. Many of these compounds are composed of substances of poor aqueous solubility. Thus, this study focused on the development of a carrier system created from biocompatible and biodegradable materials to improve the biological activity of NS extracts. Accordingly, NS was incorporated into human serum albumin template particles with MnCO3 (NS-HSA MPs) by loading NS into the preformed HAS-MnCO3 microparticles using the coprecipitation crosslinking dissolution technique (CCD-technique). After crosslinking and template dissolution steps, the NS loaded HSA particles are negatively charged, have a size ranging from 0.8 to 0.9 µm, and are peanut shaped. The degree of encapsulation efficiency ranged from 7% to 57% depending on the initial NS concentration and the steps of adsorption. In addition, NS-HSA MPs were taken up by human lung adenocarcinoma (A549 cell) for 24 h. The promotion of cellular uptake was evaluated by flow cytometry and the results produced 99% fluorescent stained cells. Moreover, the results from CLSM and 3D fluorescence imaging confirmed particle localization in the cells. Interestingly, NS-HSA MPs could not induce inflammation through nitric oxide production from macrophage RAW264.7 cells. This is the first study involving the loading of non-sericin extracts into HSA MPs by CCD technique to enhance the bioavailability and biological effects of NS. Therefore, HSA MPs could be utilized as a carrier system for hydrophobic substances targeting cells with albumin receptors.

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 Carbon Dots from Grilled Spanish Mackerel with Human Serum Albumin, γ-Globulin and Fibrinogen

Foods ◽  
2021 ◽  
Vol 10 (10) ◽  
pp. 2336
Author(s):  
Guoxin Cui ◽  
Yukun Song ◽  
Kangjing Liu ◽  
Mingqian Tan
Keyword(s):  
Human Serum Albumin ◽  
Serum Albumin ◽  
Human Serum ◽  
Carbon Dots ◽  
Plasma Proteins ◽  
Biological Effects ◽  
Human Fibrinogen ◽  
Saturation State ◽  
Spanish Mackerel ◽  
Daily Diet

The potential biological effects of food-borne carbon dots (FCDs) generated during food heating procedures on human health has received great attention. The FCDs will be inevitably exposed to blood proteins along with our daily diet to produce unknown biological effects. In this study, the interaction between FCDs extracted from grilled Spanish mackerel and three main types of human plasma proteins including human serum albumin (HSA), human γ-globulin (HGG) and human fibrinogen (HF) was reported. It was found that the grilled Spanish mackerel FCDs could affect the morphology, size and surface electrical properties of the three proteins. The interaction between the FCDs and proteins had different effects on the secondary structure of the three proteins through a static mechanism. The tested HSA, HGG, and HF could adsorb FCDs to reach saturation state within 0.5 min after the adsorption happened. The binding affinity of the FCDs to the plasma proteins was sorted as follows: HF > HGG > HSA. The results of FCDs interacted with plasma proteins provided useful information in the assessment of the safety of FCDs in our daily diet.

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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