Affinity of rosmarinic acid to human serum albumin and its effect on protein conformation stability

Peng, Xin; Wang, Xiangchao; Qi, Wei; Su, Rongxin; He, Zhimin

doi:10.1016/j.foodchem.2015.06.109

Cited by 136 publications

(67 citation statements)

References 36 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…To understand the role of tyrosine and tryptophan residues in the interaction process between HSA and drugs, HSA fluorescence excited at 280 nm and 295 nm was investigated. When an excitation wavelength of 280 nm is used, HSA fluorescence is caused by both tyrosine and tryptophan residues, whereas the 295 nm wavelength excites only the tryptophan residue . The F/F 0 plots (F 0 is the fluorescence before exposition to the quencher, F is the fluorescence after adding a quencher) against [drug]/[HSA] ratio are displayed in Figure .…”

Section: Resultsmentioning

confidence: 99%

“…Binding parameters represent very important tools in the study of pharmacokinetics and pharmacodynamics of drugs, even the metabolic modification of ligands . The binding constant ( K b ) and the number of binding sites ( n ) can be determined using the double logarithm equation:

log ([],, ((),, F_{0} - F) true/ F) = log K_{b} + n log ([],, D)

where F 0 and F are the fluorescence intensities of the systems in the absence or presence of the compound; [D] is the drug concentration; K b is the binding constant of a compound with HSA and n is the number of binding sites.…”

Section: Resultsmentioning

confidence: 99%

See 1 more Smart Citation

Influence of quercetin on the interaction of gliclazide with human serum albumin – spectroscopic and docking approaches

et al. 2017

View full text Add to dashboard Cite

Protein-binding interactions are displacement reactions which have been implicated as the causative mechanisms in many drug-drug interactions. Thus, the aim of presented study was to analyse human serum albumin-binding displacement interaction between two ligands, hypoglycaemic drug gliclazide and widely distributed plant flavonoid quercetin. Fluorescence analysis was used in order to investigate the effect of substances on intrinsic fluorescence of human serum albumin (HSA) and to define binding and quenching properties of ligand-albumin complexes in binary and ternary systems, respectively. Both ligands showed the ability to bind to HSA, although to a different extent. The displacement effect of one ligand from HSA by the other one has been described on the basis of the quenching curves and binding constants comparison for the binary and ternary systems. According to the fluorescence data analysis, gliclazide presents a substance with a lower binding capacity towards HSA compared with quercetin. Results also showed that the presence of quercetin hindered the interaction between HSA and gliclazide, as the binding constant for gliclazide in the ternary system was remarkably lower compared with the binary system. This finding indicates a possibility for an increase in the non-bound fraction of gliclazide which can lead to its more significant hypoglycaemic effect. Additionally, secondary and tertiary structure conformational alterations of HSA upon binding of both ligands were investigated using synchronous fluorescence, circular dichroism and FT-IR. Experimental data were complemented with molecular docking studies. Obtained results provide beneficial information about possible interference upon simultaneous co-administration of the food/dietary supplement and drug.

show abstract

Section: Resultsmentioning

confidence: 99%

log ([],, ((),, F_{0} - F) true/ F) = log K_{b} + n log ([],, D)

Section: Resultsmentioning

confidence: 99%

Influence of quercetin on the interaction of gliclazide with human serum albumin – spectroscopic and docking approaches

et al. 2017

View full text Add to dashboard Cite

show abstract

“…Hence, rosmarinic is accepted to be one of the most promising food-functional polyphenol. [72] Apigenin (5), a well-known metabolite found in many fruits, vegetables, and herbs, has a broad variety biological effects including, various cancer types, antioxidant, and antiinflammatory. [73] Origanum minutiflorum has a potency to be a promising medicinal plant for food and pharmaceutical industries on account of including significant bioactive compounds.…”

Section: Resultsmentioning

confidence: 99%

Antioxidant activity of an anatolian herbal tea—Origanum minutiflorum: isolation and characterization of its secondary metabolites

Elmastaş

Celik

Genç

et al. 2018

International Journal of Food Properties

View full text Add to dashboard Cite

Origanum species are significant aromatic and medicinal plants used in food and pharmaceutical industries. Isolation of bioactive compounds was executed on n-butanol extract to yield the compounds responsible for the activities. Tricosan-1-ol (1), (8E,16E)-tetracosa-8,16-diene-1,24-diol (2), azepan-2-one (3), 3,4-dihydroxybenzoic acid (4), apigenin (5), eriodictyol (6), globoidnan-A (7), luteolin (8), rosmarinic acid (9), apigenin-7-O-glucuronide (10), and vicenin-2 (11) were isolated by chromatographic methods (column chromatography and semi-preparative High Performance Liquid Chromatography (HPLC) and structures were elucidated on the basis of spectroscopic techniques including 1D/2D nuclear magnetic resonance (NMR) and Liquid chromatography/Time-of-flight/Mass spectrometry (LC-TOF/MS). The isolated compounds and extracts were applied for antioxidant assays including 1,1-diphenyl-2-picrylhydrazyl (DPPH • ) scavenging, 2,2'-azino-bis(3-ethylbenzothiazoline-6-sulphonic acid) (ABTS •+ ) scavenging, reducing power, and cuprac techniques. 3,4-Dihydroxy benzoic acid (4), eriodictyol (6), luteolin (8), and rosmarinic acid (9) revealed the considerable antioxidant activities. ARTICLE HISTORY

show abstract

“…A previous study indicated that there are three main regions in HSA for ligand binding, namely Sudlow's site I in subdomain IIA, site II in subdomain IIIA, and site III, which was independent of sites I and II. The specific site markers warfarin, ibuprofen, and digitoxin, which were reported to bind to site I, site II, and site III of HSA, respectively, were selected to conduct the site displacement studies . In this experiment, site markers were gradually added to the QY and HSA solution, keeping the concentration ratio at 4:1 to minimise nonspecific binding of the site marker .…”

Section: Resultsmentioning

confidence: 99%

Interaction between quinoline yellow and human serum albumin: spectroscopic, chemometric and molecular docking studies

Wang

Pan

et al. 2018

J Sci Food Agric

View full text Add to dashboard Cite

show abstract

Affinity of rosmarinic acid to human serum albumin and its effect on protein conformation stability

Cited by 136 publications

References 36 publications

Influence of quercetin on the interaction of gliclazide with human serum albumin – spectroscopic and docking approaches

Influence of quercetin on the interaction of gliclazide with human serum albumin – spectroscopic and docking approaches

Antioxidant activity of an anatolian herbal tea—Origanum minutiflorum: isolation and characterization of its secondary metabolites

Interaction between quinoline yellow and human serum albumin: spectroscopic, chemometric and molecular docking studies

Contact Info

Product

Resources

About