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

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.

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Neurokinin receptor mediated plasma extravasation in guinea pig and rat airways: comparison of 125I-labelled human fibrinogen and 99mTc-labelIed human serum albumin as markers of leakage

Canadian Journal of Physiology and Pharmacology ◽

10.1139/y93-073 ◽

1993 ◽

Vol 71 (7) ◽

pp. 506-511 ◽

Cited By ~ 6

Author(s):

Christine Tousignant ◽

Chi-Chung Chan ◽

Donna Young ◽

Diane Guevremont ◽

Ian W. Rodger

Keyword(s):

Human Serum Albumin ◽

Guinea Pig ◽

Serum Albumin ◽

Human Serum ◽

Plasma Extravasation ◽

Human Fibrinogen ◽

Protein Extravasation ◽

Neurokinin Receptor ◽

Lower Airways ◽

Dose Dependent

In the present study we have characterized NK-1 and NK-2 receptor induced microvascular leakage in guinea pig and rat airways, using 125I-labelled human fibrinogen ([125I]FN) versus 99mTc-labelled human serum albumin ([99mTc]HSA) as markers for plasma protein extravasation. Intravenous administration of the selective NK-1 agonist [Sar9, Met(O2)11]SP (1 nmol kg−1) caused a dose-dependent increase of [125I]FN extravasation in guinea pig trachea, main bronchi, secondary bronchi, and intraparenchymal airways. Extravasation of [125I]FN increased by up to 192 (trachea), 284 (main bronchi), 368 (secondary bronchi), and 271% (intraparenchymal bronchi) over control levels in these regions of the airways. Pretreatment of the animals with CP 99,994 and RP 67,580, two NK-1 nonpeptide antagonists, caused a dose-dependent inhibition of [Sar9, Met(O2)11]SP-induced leakage of [125I]FN. [Sar9, Met(O2)11]SP (1 nmol kg−1) did not induce specific leakage of [99mTc]HSA in the intraparenchymal bronchi. Specific NK-2 receptor induced leakage was detected in the lower airways but only when using [125I]FN as a marker. We have also compared the ability of CP 99,994 and RP 67,580 to inhibit [Sar9, Met(O2)11]SP induced extravasation of [125I]FN in rat airways. CP 99,994 was 40–50 (tracheobronchial region) to 75 (lower airways) times more potent in the guinea pig than the rat airways. In contrast, RP 67,580 had higher affinity for rat airways compared with guinea pig airways. The results of this study highlight the superiority of [125I]FN as a sensitive marker of plasma extravasation over [99mTc]HSA. Furthermore, the results strongly suggest that both NK-1 and NK-2 receptors mediate plasma extravasation in the guinea pig lower airways and that NK-1 receptors are different in guinea pig and rat airways.Key words: Leakage, tachykinins, NK-1 and NK-2 receptors, airway, asthma.

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Influence of Human Serum Albumin Glycation on the Binding Affinities for Natural Flavonoids

Open Chemistry ◽

10.1515/chem-2019-0079 ◽

2019 ◽

Vol 17 (1) ◽

pp. 806-812

Author(s):

Liangliang Liu ◽

Yi Liu ◽

Aiping Xiao ◽

Shiyong Mei ◽

Yixi Xie

Keyword(s):

Human Serum Albumin ◽

Serum Albumin ◽

Human Serum ◽

Small Molecules ◽

Human Body ◽

Binding Sites ◽

Plasma Proteins ◽

Fluorescence Spectra ◽

Binding Affinities ◽

Dietary Flavonoids

AbstractIncreasing the degree of glycation in diabetes could affect the ability of plasma proteins in binding to small molecules and active compounds. In this study, the influence of glycation of Human serum albumin (HSA) on the binding affinities for six dietary flavonoids was investigated by fluorescence spectra. Glycated HSA was prepared through incubation with glucose and characterized by several methods to confirm the glycation. It was found that the level of glycation increased with the increasing incubation time. The glycation of HSA increased the binding affinities for flavonoids by 1.40 to 48.42 times, which indicates that modifications caused by the glycation may have different influences on the interactions of flavonoids with HSA at separate binding sites on this protein. These results are valuable for understanding the influence of diabetes on the metabolism of flavonoids and other bioactive small molecules in human body.

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Toxicity Alleviation of Carbon Dots from Roast Beef after the Formation of Protein Coronas with Human Serum Albumin

Journal of Agricultural and Food Chemistry ◽

10.1021/acs.jafc.0c03499 ◽

2020 ◽

Vol 68 (36) ◽

pp. 9789-9795 ◽

Cited By ~ 1

Author(s):

Kangjing Liu ◽

Yukun Song ◽

Mingqian Tan

Keyword(s):

Human Serum Albumin ◽

Serum Albumin ◽

Human Serum ◽

Carbon Dots ◽

Roast Beef

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Binding of Testosterone and Oestradiol to Sex Hormone Binding Globulin, Human Serum Albumin and other Plasma Proteins: Evidence for Non-Specific Binding of Oestradiol to Sex Hormone Binding Globulin

Clinical Science ◽

10.1042/cs0640307 ◽

1983 ◽

Vol 64 (3) ◽

pp. 307-314 ◽

Cited By ~ 29

Author(s):

M. Jawed Iqbal ◽

Maureen Dalton ◽

Robert S. Sawers

Keyword(s):

Human Serum Albumin ◽

Serum Albumin ◽

Human Serum ◽

Binding Site ◽

Plasma Proteins ◽

Specific Binding ◽

Sex Hormone ◽

Sex Hormone Binding Globulin ◽

Normal Female ◽

Hormone Binding

1. The percentage binding of testosterone (T) and oestradiol (E2) to sex hormone binding globulin (SHBG) and human serum albumin (HSA) was determined over a range of SHBG concentrations of 16–250 nmol of dihydrotestosterone (DHT) bound/l. It was found that the binding of both T and E2 to HSA was a function of their binding to SHBG and bore an inverse relationship to it. After removal of both SHBG and HSA from plasma by affinity chromatography a ‘residual’ binding of about 11% for T and 12% for E2 was still apparent. in addition to the specific high-affinity, low capacity binding of E2 to SHBG, non-specific low-affinity binding of 7–12% was demonstrated after selective denaturation of the specific binding site of the latter. 2. Competition studies indicated that although at the relatively higher levels of SHBG found in the normal female the physiological concentrations of E2, T and DHT need not be taken into account in estimating the unbound fractions of steroids, at the relatively lower levels of SHBG found in normal men and hirsute women, the physiological concentrations of T and DHT are effective in causing statistically significant displacement of E2 from the common, specific binding site on SHBG. 3. A simple computerized technique is described for the determination of fractions of E2 and T respectively, that are unbound to SHBG, unbound to SHBG and HSA, and unbound to all plasma proteins, when the total plasma levels of E2, T, DHT and SHBG are known.

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Systematical investigation of in vitro molecular interaction between fluorescent carbon dots and human serum albumin

RSC Advances ◽

10.1039/c6ra01386d ◽

2016 ◽

Vol 6 (50) ◽

pp. 44531-44542 ◽

Cited By ~ 28

Author(s):

Shan Huang ◽

Hangna Qiu ◽

Jiangning Xie ◽

Chusheng Huang ◽

Wei Su ◽

...

Keyword(s):

Human Serum Albumin ◽

Serum Albumin ◽

Human Serum ◽

Molecular Interaction ◽

Carbon Dots ◽

Electrochemical Techniques ◽

Fluorescent Carbon Dots ◽

Fluorescent Carbon

In vitro molecular interaction between fluorescent CDs and HSA was systematically investigated by multispectroscopic and electrochemical techniques.

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Interaction of plasma proteins with cytochromes P450 mediated metabolic reactions: inhibition by human serum albumin and α-globulins of the debrisoquine 4-hydroxylation (CYP2D) in liver microsomes of human, hamster and rat

Toxicology Letters ◽

10.1016/s0378-4274(01)00264-8 ◽

2001 ◽

Vol 119 (3) ◽

pp. 219-225 ◽

Cited By ~ 11

Author(s):

Mikio Ishii ◽

Bang Q Xu ◽

Li R Ding ◽

Nancy E Fischer ◽

Tadanobu Inaba

Keyword(s):

Human Serum Albumin ◽

Serum Albumin ◽

Human Serum ◽

Plasma Proteins ◽

Cytochromes P450 ◽

Liver Microsomes ◽

Metabolic Reactions

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In-vitro molecular interaction of boron doped carbon dots with human serum albumin

IOP Conference Series Materials Science and Engineering ◽

10.1088/1757-899x/1120/1/012012 ◽

2021 ◽

Vol 1120 (1) ◽

pp. 012012

Author(s):

Vinayak Sahu ◽

Fahmida Khan ◽

Pradeep Kumar Dewangan ◽

Komal Kashyap ◽

Sonalika Agrawal ◽

...

Keyword(s):

Human Serum Albumin ◽

Serum Albumin ◽

Human Serum ◽

Molecular Interaction ◽

Carbon Dots ◽

Boron Doped ◽

Doped Carbon Dots

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A novel 3D-printed centrifugal ultrafiltration method reveals in vivo glycation of human serum albumin decreases its binding affinity for zinc

Metallomics ◽

10.1039/d0mt00123f ◽

2020 ◽

Vol 12 (7) ◽

pp. 1036-1043 ◽

Cited By ~ 1

Author(s):

Monica J. Jacobs ◽

Cody W. Pinger ◽

Andre D. Castiaux ◽

Konnor J. Maloney ◽

Dana M. Spence

Keyword(s):

Human Serum Albumin ◽

Serum Albumin ◽

Human Serum ◽

High Glucose ◽

Plasma Proteins ◽

Structure And Function ◽

3D Printed ◽

And Function ◽

Centrifugal Ultrafiltration

Plasma proteins are covalently modified in vivo by the high-glucose conditions in the bloodstreams of people with diabetes, resulting in changes to both structure and function.

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A study on human serum albumin corona formed on photoluminescent carbon dots

Journal of Chemical Research ◽

10.1177/1747519819895710 ◽

2020 ◽

Vol 44 (7-8) ◽

pp. 447-452

Author(s):

Peng Wang ◽

Ming Yuan ◽

Na Li ◽

Feng Zhang

Keyword(s):

Human Serum Albumin ◽

Serum Albumin ◽

Human Serum ◽

Carbon Dots ◽

Resonance Energy ◽

Binding Constants ◽

Protein Corona ◽

Hybrid Nanomaterial ◽

Corona Formation ◽

Biomedical Field

Fluorescence nanostructures have been widely applied in the biomedical field as therapeutic agents and as novel tools for labeling, imaging, and sensing. However, the protein corona will dramatically influence the predesigned properties of nanostructures in serum. Therefore, it is important to understand the mechanism of protein corona formation on nanostructures. Photoluminescent carbon dots have been widely applied in the biomedical field since their discovery. Due to the large overlap between the absorption spectra of proteins and the fluorescence spectra of photoluminescent carbon dots, herein we investigate the mechanism of human serum albumin corona formed on photoluminescent carbon dots using fluorescence resonance energy transfer. By employing spectroscopic methods, the binding constants and the number of binding sites between human serum albumin and photoluminescent carbon dots have been determined, and the corresponding thermodynamics are also discussed as well for the interaction between photoluminescent carbon dots and human serum albumin. In addition, we successfully demonstrate the photoluminescent carbon dots in labeling bean sprouts. We believe that the current research cannot shed light on the mechanism of protein corona formation on nanostructures, but also could benefit the design of hybrid nanomaterial which will be applied to serum environments.

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