The study on the interaction between human serum albumin and a new reagent with antitumour activity by spectrophotometric methods

Gao, Hong; Lei, Liandi; Liu, Jiaqin; Kong, Qin; Chen, Xingguo; Hu, Zhide

doi:10.1016/j.jphotochem.2004.05.017

Cited by 267 publications

(103 citation statements)

References 24 publications

Supporting

Mentioning

100

Contrasting

Unclassified

Order By: Relevance

“…Thus, it is important to understand not only how much drug is bound to protein, but also the site-specificity and the nature of forces involved in the binding of these agents with serum albumin, the major drug binding protein in blood plasma. Fluorescence spectroscopy, due to its exceptional sensitivity, selectivity and sound theoretical foundation [6], is a convenient method for studying drug-protein interaction [7][8]. In the present work, the mechanism of interaction and detailed physico-chemical characterization of the binding of glimepiride and glipizide with human serum albumin Mechanism of interaction of hypoglycemic agents glimepiride and glipizide with human serum albumin has been studied using fluorescence spectroscopy.…”

Section: Introductionmentioning

confidence: 99%

Mechanism of interaction of hypoglycemic agents glimepiride and glipizide with human serum albumin

Seedher

Kanojia

2009

Open Chemistry

View full text Add to dashboard Cite

Abstract:The mechanism of interaction of hypoglycemic drugs, glimepiride and glipizide with human serum albumin (HSA) has been studied using fluorescence spectroscopy. The results are discussed in terms of the binding parameters, thermodynamics of the binding process, nature of forces involved in the interaction, identification of drug binding site on serum albumin and the fluorescence quenching mechanism involved. The association constants were of the order of 10 5 and glipizide was found to have much higher affinity for HSA than glimepiride at all temperatures. Thermodynamic parameters for the binding suggested that hydrophobic interactions are primarily involved in the binding of these drugs to HSA. However, glimepiride and glipizide appear to cause temperature-dependent conformational changes in the albumin molecule and, therefore, the nature of interaction varied with temperature. Glimepiride and glipizide bind to both site I and site II on HSA, but the primary interaction occurs at site II. The binding region in site II is different for the two drugs. Stern-Volmer analysis of quenching data indicated that tryptophan residues of HSA are not fully accessible to the drugs and a predominantly dynamic quenching mechanism is involved in the binding. Results can provide useful insight into prediction of competitive displacement of these drugs by other co-administered drugs and excipients, resulting in serious fluctuations of the blood glucose levels in diabetic patients.

show abstract

Section: Introductionmentioning

confidence: 99%

Mechanism of interaction of hypoglycemic agents glimepiride and glipizide with human serum albumin

Seedher

Kanojia

2009

Open Chemistry

View full text Add to dashboard Cite

show abstract

“…4) These results provide salient information of the structural features that determine the therapeutic effectiveness of drugs, and hence become an important research field in chemistry, life sciences and clinical medicine. 1,[4][5][6][7][8] Two common methods that have been used in evaluating the binding of drugs to albumin include equilibrium dialysis and ultrafiltration. 9,10) These methods are laborious and time consuming and the results at times are not reproducible.…”

mentioning

confidence: 99%

“…6) The CD results were expressed in terms of mean residue ellipticity (MRE) in deg cm 2 dmol Ϫ1 according to the following equation, (12) where C P is the molar concentration of the protein, n is the number of aminoacid residues and l is the path length. The a-helical contents of free and combined BSA 7) were calculated from MRE value at 208 nm using the equation (13) where MRE 208 is the observed MRE value at 208 nm, 4000 is the MRE of the b-form and random coil conformation cross at 208 nm, and 33000 is the MRE value of a pure a-helix at 208 nm. From the above equation, the quantitative analysis results of the a-helix in the secondary structure of BSA were obtained.…”

mentioning

confidence: 99%

Spectroscopic Studies and Life Time Measurements of Binding of a Bioactive Compound to Bovine Serum Albumin and the Effects of Common Ions and Other Drugs on Binding

Shaikh

Seetharamappa

Ashoka

et al. 2006

CHEMICAL & PHARMACEUTICAL BULLETIN

View full text Add to dashboard Cite

The interaction of a drug with blood components influences its bioavailability and can affect the functions of several biomolecules.1) Clinical effect of the plasmatic level of a drug is an important pharmacological parameter determined by drug absorption, distribution and elimination. Serum albumins, the most abundant proteins in circulatory system of a wide variety of organisms, have been well studied for many years. They account for about 60% of the total protein corresponding to a concentration of 42 g l Ϫ1 2,3) and provide about 80% of osmotic pressure of blood.2) Albumins have been used as a model protein for diverse biophysical, biochemical and physicochemical studies 3) to gain general fundamental insights into drug-protein binding. The remarkable binding properties of albumin accounts for the central role it can play in both the efficacy and rate of delivery of drugs. Several classes of drugs including tranquillizers, anti-coagulants and general anesthetics are transported in the blood while bound to albumin. This kind of work has stimulated many researchers to carry out the research on the nature of the drug binding sites and investigations of whether natural metabolites, drugs and fatty acids compete with one another for binding to the protein. 4) These results provide salient information of the structural features that determine the therapeutic effectiveness of drugs, and hence become an important research field in chemistry, life sciences and clinical medicine. 1,[4][5][6][7][8] Two common methods that have been used in evaluating the binding of drugs to albumin include equilibrium dialysis and ultrafiltration.9,10) These methods are laborious and time consuming and the results at times are not reproducible. However, these conventional methods are often inapplicable to the analyses of strongly bound drugs because of technical problems such as drug adsorption on the membrane and the leakage of bound drug through membrane. To overcome these problems, we have employed fluorimetric, lifetime measurements, absorption and circular dichroism methods to investigate the mode of binding of NIM with BSA in the present investigation.Nimesulide (NIM), chemically N-(4-nitro-2-phenoxyphenyl) methanesulphonamide, is a relatively new non-steroidal antiinflammatory (NSAID), antipyretic and analgesic drug. 11)It is widely used for the treatment of inflammatory conditions associated with rheumatoid arthritis, respiratory tract infections, soft tissue and oral cavity inflammations. The therapeutic effect of NSAIDs is the result of their ability to inhibit prostaglandin synthesis via inhibition of cyclooxigenase. The analgesic potency of NIM is similar to that of ibuprofen and indomethacin. Nonetheless, NIM has shown a higher antipyretic potency relatively than indomethacin, ibuprofen, aspirin and paracetamol. Because of its biological importance, we thought of investigating the mechanism of binding of NIM with BSA by fluorescence, UV-visible absorption, circular dichroism and fluorescence lifetime measurements. The ener...

show abstract

“…Dynamic and static quenching can be distinguished by their differing dependence on temperature and viscosity, or preferably by lifetime measurements. Higher temperatures result in faster diffusion and hence increased dynamic quenching; in contrast, higher temperatures will typically result in the dissociation of weakly bound complexes, and decreased static quenching [35]. The results showed that the values of K SV and K b constants for Q and AA decreased with increasing temperature.…”

Section: Fluorescence Quenching Mechanism and Determination Of Bindinmentioning

confidence: 92%

“…The apparent binding constant (K b ) and number of binding sites (n) can be calculated using the following equation [35]:…”

Section: Fluorescence Quenching Mechanism and Determination Of Bindinmentioning

confidence: 99%

Interactions of Bioactive Quince (Cydonia oblonga Mill.) Extract with Biomolecules

Strugała¹,

Cyboran-Mikołajczyk²,

Wyspiańska³

et al. 2017

Rec. Nat. Prod.

View full text Add to dashboard Cite

Abstract:The study is concerned with biological activity of quince (Q) fruit extract (Cydonia oblonga Mill.) towards the phosphatidylcholine liposome and the natural lipid-protein erythrocyte membrane, as well as will explaining the40 way of interaction of the extract with the membrane. The results showed that Q extract protects lipids against oxidation induced by AAPH compound to a similar extent in two models of membrane. Studies with probes (Laurdan and DPH) located at different depths within the membrane lipid bilayer showed that extract caused an increase of the packing order of the polar heads of lipids and a slight decrease in mobility of the acyl chains. Such results suggest that extract molecules associate with the lipid and lipid-protein membrane and can stop the propagation of free radicals within the bilayer by modifying the membrane fluidity. Furthermore, Q extract resulted in the inhibition of the activity of enzymes (cyclooxygenase-1 and cyclooxygenase-2) probably involved in inflammatory reactions in the body. The experimental results proved that extract components can bind to the main plasma protein -human serum albumin, and the quenching mechanism was suggested as static. The obtained quince-albumin binding constants show that the extract probably can be transported from the circulatory system to reach its target organ.

show abstract

The study on the interaction between human serum albumin and a new reagent with antitumour activity by spectrophotometric methods

Cited by 267 publications

References 24 publications

Mechanism of interaction of hypoglycemic agents glimepiride and glipizide with human serum albumin

Mechanism of interaction of hypoglycemic agents glimepiride and glipizide with human serum albumin

Spectroscopic Studies and Life Time Measurements of Binding of a Bioactive Compound to Bovine Serum Albumin and the Effects of Common Ions and Other Drugs on Binding

Interactions of Bioactive Quince (Cydonia oblonga Mill.) Extract with Biomolecules

Contact Info

Product

Resources

About