Fluorescence spectroscopy of osthole binding to human serum albumin

Yang, Guangde; Liu, Cong; Zeng, Aiguo; Zhao, Yuan; Yang, Rong; Bian, Xiaoli

doi:10.1016/j.jpha.2012.10.002

Cited by 27 publications

(25 citation statements)

References 19 publications

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“…The fluorescence intensity of HSA was quenched by the addition of NPs indicating binding between NPs and HAS . After 5 min of incubation, the largest decrease in HSA maximum fluorescence intensity was exhibited by non‐PEGylated NPs ( P < 0.05).…”

Section: Resultsmentioning

confidence: 99%

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Influence of PEGylation on PLGA nanoparticle properties, hydrophobic drug release and interactions with human serum albumin

Samkange

D’Souza

Obikeze

et al. 2019

Journal of Pharmacy and Pharmacology

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Objective To evaluate the impact of PEG content on poly(lactic‐co‐glycolic acid) (PLGA) NP physicochemical properties, hydrophobic drug release (rifampicin as a model drug) and human serum protein binding. Methods Rifampicin loaded and unloaded nanoparticles with PEG content of 0–17% (w/w) were prepared by an emulsification–evaporation technique. Nanoparticles were characterized for size, zeta potential and morphology. PEGlyation was confirmed using proton nuclear magnetic resonance (1H NMR). Fluorescence spectroscopy and dynamic light scattering were used to determine nanoparticle‐protein binding, binding constants and stability of nanoparticles in human serum, respectively. Drug loading and release were determined by UV‐VIS spectroscopy and drug release data was mathematically modelled. Key findings A NP PEG content of 17% w/w significantly retarded release of rifampicin from PLGA NPs and altered kinetics of drug release. Stern–Volmer (Ksv) protein binding constants decreased upon PEG incorporation. A 2% w/w PEG was sufficient to significantly reduce protein binding extent to PLGA NPs and maintain particle size distributions. Conclusion The ability to fine tune drug release and formation of protein corona around nanoparticles is crucial to formulation scientists. This study suggests that PLGA NPs with low PEG content might be suitable for extended circulation and rapid drug release and that higher PEG content retards hydrophobic drug release.

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Section: Resultsmentioning

confidence: 99%

“…To evaluate the influence of PEG content on human serum albumin (HSA) NP binding, a fluorescence quenching technique was used . NPs with a concentration of 1 mg/ml were incubated in 55% (v/v) human serum at 37°C for set time points (5, 20 and 60 min).…”

Section: Methodsmentioning

confidence: 99%

Influence of PEGylation on PLGA nanoparticle properties, hydrophobic drug release and interactions with human serum albumin

Samkange

D’Souza

Obikeze

et al. 2019

Journal of Pharmacy and Pharmacology

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show abstract

“…Serum albumins, widely studied transport proteins are abundantly found in blood plasma [1][2][3][4][5][6][7][8][9][10][11][12]. Besides being an attractive macromolecular carrier, serum albumins play a vital role by increasing the solubility of hydrophobic drugs in the blood plasma, binding with bio-active molecules and maintaining colloid blood pressure [3,4].…”

Section: Introductionmentioning

confidence: 99%

“…As many bioactive small molecules bind reversibly to serum albumins, it is important to study the interactions of drugs with this protein as these studies can provide information about the structural features that determine the therapeutic effect of drugs and have become an interesting research field in life science, chemistry and clinical medicine. The study regarding the mode of binding of various molecules to serum albumins is chiefly accountable for the understanding of metabolism, bio-distribution, elimination or pharmacological effects of the drugs in the body [5][6][7][8][9][10][11][12][14][15][16][17][18][19][20][21][22][23][24][25][26]. Knowledge of interaction mechanisms between endogenous and exogenous molecules and plasma proteins has a great value for researchers to understand the pharmacodynamics and pharmacokinetics of a drug candidate.…”

Section: Introductionmentioning

confidence: 99%

Constrained Photophysics of 5,7-dimethoxy-2,3,4,9-tetrahydro-1H-carbazol-1-one in the Bioenvironment of Serum Albumins: A Spectroscopic Endeavour Supported by Molecular Docking Analysis

Mitra

Pal

et al. 2017

J Fluoresc

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This paper vividly indicates that steady state as well as time-resolved fluorescence techniques can serve as highly sensitive monitors to explore the interactions of 5,7-dimethoxy-2,3,4,9-tetrahydro-1H-carbazol-1-one with model transport proteins, bovine serum albumin (BSA) and human serum albumin (HSA). Besides these, we have used fluorescence anisotropy study to assess the degree of restrictions imparted by the micro-environments of serum albumins. Again, to speculate the triplet excited state interaction between such fluorophore and albumin proteins (BSA& HSA), laser flash-photolysis experiments have been carried out. Molecular docking experiments have also been performed to support the conclusions obtained from steady state experiments.

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“…The binding capacity of a drug to serum albumin present in human blood has momentous effect on metabolism of drugs throughout the human body [7]. Several commercially prepared protein assay reagents are already available, and for our work, we have used the Lowry's reagent [8].…”

Section: Introductionmentioning

confidence: 99%

Effect of Ampicillin and Chloramphenicol on Chick Serum

Nanda

Suneetha

2017

Asian J Pharm Clin Res

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Objective: Cystatin protein present in chick serum exhibits antimicrobial activity. The present study focuses on the effect of ampicillin and chloramphenicol antibiotics on chick serum and thus verifies Beer-Lambert's law. Methods:The serum is separated from the cellular matter with the help of a micropipette to get a clean serum sample. The quantification of protein was done by Lowry's method. The antibiotics ampicillin and chloramphenicol stock solution were prepared by 10 mg of antibiotic powder in 10 ml of sterilized water. The statistical analysis of the values obtained was done by SPSS logistics software. Results:The different values of concentration of serum with absorption showed a linear relationship which verifies Beer-Lambert's law. With an increase in the concentration of protein in chick serum, the absorption also increases, which gives a range of concentration of protein at which ampicillin and chloramphenicol act. Conclusion:The rise and fall in the absorbance rate of proteins after addition of different antibiotics represent the increase and decrease in the concentration of proteins, respectively. This shows that every antibiotic acts at a particular concentration on the protein of the serum. Therefore, proper doses of antibiotics are recommended by the doctors.

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Fluorescence spectroscopy of osthole binding to human serum albumin

Cited by 27 publications

References 19 publications

Influence of PEGylation on PLGA nanoparticle properties, hydrophobic drug release and interactions with human serum albumin

Influence of PEGylation on PLGA nanoparticle properties, hydrophobic drug release and interactions with human serum albumin

Constrained Photophysics of 5,7-dimethoxy-2,3,4,9-tetrahydro-1H-carbazol-1-one in the Bioenvironment of Serum Albumins: A Spectroscopic Endeavour Supported by Molecular Docking Analysis

Effect of Ampicillin and Chloramphenicol on Chick Serum

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