Fluorescence Studies on the Interactions of Barbaloin with Bovine Serum Albumin

Tian, Jianniao; Liu, Jiaqin; Zhang, Jiyou; Hu, Zhide; Chen, Xinguo

doi:10.1248/cpb.51.579

Cited by 98 publications

(50 citation statements)

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“…However, the information on the indirubin-BSA binding mode, the binding constant, and the effects of indirubin complexation on the protein secondary structure is obscure. 17) In this work, we report the fluorescence, UV-Vis and FT-IR spectroscopic results on the binding of indirubin to BSA in aqueous solutions at physiological pH. Spectroscopic evidence regarding the drug binding mode, binding constant, and the change of protein secondary structure is described.…”

mentioning

confidence: 97%

Study of the Interaction of Indirubin with Bovine Serum Albumin

Bian

et al. 2006

CHEMICAL & PHARMACEUTICAL BULLETIN

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Indirubin (2H-indol-2-one, 3-(1,3-dihydro-3-oxo-2H-indol-2-ylidene)-1,3-dilydro) constitutes the main active ingredient of a traditional Chinese medicinal recipe, Danggui Longhui Wan, used to treat various diseases including chronic myelocytic leukemia. 1,2) Indirubin is an inhibitor of cyclin dependent kinases and glycogen synthase kinase. [3][4][5] Indirubin has been recently discovered to be a potent ligand of the aryl hydrocarbon receptor (AhR), also known as the "dioxin receptor".6) Recent studies also showed that indirubin inhibits 2,4,6-trinitro-1-chlorobenzene (TNBC)-induced inflammatory reactions in mice. 7)Bovine serum albumin (BSA) is a single-chain 582 amino acid globular nonglycoprotein cross-linked with 17 cystine residues (8 disulfide bonds and 1 free thiol). As one of the most abundant proteins, BSA plays an important role in the transport and deposition of a variety of endogenous and exogenous ligands in blood. BSA is divided into three linearly arranged, structurally distinct, and evolutionarily related domains (I-III) [8][9][10][11] ; each domain is composed of two subdomains (A, B). BSA has two tryptophans embedded in two different domains, one is Trp-134, located in the proximity of the protein surface, but buried in a hydrophobic pocket of domain I, the other is Trp-214, located in an internal part of domain II.12) BSA has a wide range of physiological functions involving the binding, transport, and delivery of fatty acids, bilirubin, porphyrins, thyroxine, tryptophan and steroids. [8][9][10][11] It is home to specific binding sites for metals, pharmaceuticals, and dyes. The binding ability on the interaction of drug with protein will significantly affect the apparent distribution volume of the drugs and also affect the elimination rate of drugs in most cases; so the studies on this aspect become an important research field in life sciences, chemistry and clinical medicine because it can provide important information on the structural features which determine the therapeutic effectiveness of drugs.Serial study methods concerning the interaction between drugs and protein include NMR, 13) CD, 14) ROD, 15) Raman 16) attenuated total reflectance-Fourier transform infrared (ATR-FTIR), UV-Vis absorbance and fluorescence spectroscopy. Fluorescence quenching techniques are great aids in the study of binding of drugs to plasma proteins and serum albumin in particular because of their high sensitivity, rapidity and ease of implementation. FT-IR spectroscopy has recently become very popular for the structural characterization of proteins. The most important advantage of FT-IR spectroscopy for biological studies is that the spectra of almost any biological system can be obtained in a wide variety of environments. For secondary-structure analysis of proteins, so far, many studies have been carried out to investigate the interaction of proteins with drugs. However, the information on the indirubin-BSA binding mode, the binding constant, and the effects of indirubin complexation on the protein secondary s...

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confidence: 97%

Study of the Interaction of Indirubin with Bovine Serum Albumin

Bian

et al. 2006

CHEMICAL & PHARMACEUTICAL BULLETIN

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“…The binding constant K and the number of binding sites were taken as aparameter in this study. In addition, the thermodynamic functions enthalpy and entropy for the reaction were also carried out [27] . Patented hyper-dry system in combination of freeze-dry technique with micro wave and far infrared radiation was used for the preparation of Aloe vera high molecular weight fractions (AHM) which contain barbaloin as phytoconstituents [28] .…”

Section: Analytical Methods Of Barbaloinmentioning

confidence: 99%

Barbaloin: A concise report of its pharmacological and analytical aspects

Patel

Tahilyani³

2012

Asian Pacific Journal of Tropical Biomedicine

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“…warfarin) are known to bind extensively to blood-soluble proteins. Serum albumins, which are the major soluble protein constituents of the circulatory system (4% w/v), have the ability to reversibly bind a large variety of exogenous compounds including fatty acids, amino acids, drugs and pharmaceuticals [34][35][36]. Plasma protein binding forms an integral part of distribution and bioavailability for numerous medications currently on the market but might also become problematic where binding is extensive [37,38].…”

Section: Minimum Inhibitory Concentration Determinationmentioning

confidence: 99%

Versatility of 7-Substituted Coumarin Molecules as Antimycobacterial Agents, Neuronal Enzyme Inhibitors and Neuroprotective Agents

Kapp

Visser

Sampson

et al. 2017

Preprint

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An in vitro medium-throughput screen using M. tuberculosis H37Rv was employed to screen an in-house library of structurally diverse compounds for antimycobacterial activity. From this initial screen, eleven 7-substituted coumarin derivatives with confirmed monoamine oxidase-B and cholinesterase inhibitory activities, demonstrated growth inhibition of more than 50% at a 50 µM concentration. This prompted further exploration of all the 7-substituted coumarins in our library, nineteen in total, as potential antimycobacterial agents. Four derivatives showed promising antimycobacterial activity with MIC99 values of 8.31 -29.70 µM and 44.15 -57.17 µM on M. tuberculosis H37Rv in independent assays using Gaste-Fe and 7H9 + OADC media, respectively. These compounds were found to bind to albumin which may explain the variations in MIC between the two assays. Preliminary antimycobacterial evaluation of moxifloxacin resistant M. tuberculosis show that these compounds are able to maintain their activity in fluoroquinolone resistant mycobacteria. Analysis of structure activity relationships for antimycobacterial versus neuronal enzyme inhibitory activity indicate that structural modification on position 4 and/or 7 of the coumarin scaffold may be utilized to improve selectivity towards either inhibition of neuronal enzymes or antimycobacterial effect. Cytotoxicity evaluations of the compounds indicate moderate cytotoxicity with slight selectivity towards mycobacteria. Further neuroprotective assays on SH-SY5Y human neuroblastoma cells indicate significant neuroprotection for selected compounds irrespective of their neuronal enzyme inhibitory properties. These coumarin molecules are thus interesting lead compounds that may provide insight into the design of new antimicrobacterial and/or neuroprotective agents.

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Fluorescence Studies on the Interactions of Barbaloin with Bovine Serum Albumin

Cited by 98 publications

References 10 publications

Study of the Interaction of Indirubin with Bovine Serum Albumin

Study of the Interaction of Indirubin with Bovine Serum Albumin

Barbaloin: A concise report of its pharmacological and analytical aspects

Versatility of 7-Substituted Coumarin Molecules as Antimycobacterial Agents, Neuronal Enzyme Inhibitors and Neuroprotective Agents

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