Disease relevance of Phenylperi acid

• Detection of ATP-dependent conformational change in the F1 portion and beta subunit of Escherichia coli H+-ATPase using 8-anilinonaphthalene-1-sulfonate [1].
• The conformation of beta-lactamase I from Bacillus cereus was examined over the pH 1.5-12.5 region by circular dichroism (CD), tryptophan fluorescence, dynamic light scattering, and 1-anilino-8-naphthalenesulfonate (ANS) binding [2].
• Media containing the fluorogenic compound 8-anilino-1-naphthalene sulfonic acid may be used to discriminate between gram-positive and gram-negative bacteria and to differentiate between various species of bacteria [3].
• Acid-induced unfolding of the tetrameric glucose/xylose isomerase (GXI) from Streptomyces sp. NCIM 2730 has been investigated using intrinsic fluorescence, fluorescence quenching, second derivative spectroscopy, hydrophobic dye (1-anilino-8-naphthalene-sulfonate) binding and CD techniques [4].
• Biodegradation of 8-anilino-1-naphthalenesulfonic acid by Pseudomonas aeruginosa [5].

High impact information on Phenylperi acid

• The binding of TF1 to TF0 present in vesicles restored energy-transducing activities, such as ATP-32Pi exchange, dicyclohexylcarbodiimide-sensitive ATPase, and ATP-dependent enhancement of 8-anilinonaphthalene-1-sulfonate fluorescence [6].
• Furthermore, a large increase in fluorescence (>50-fold) is observed upon the addition of pVHL into a solution containing 8-anilino-1-naphthalene sulfonic acid [7].
• We examined the kinetics of fibrillogenesis using three techniques: the time dependence of the fluorescence emission of thioflavin T and 1-anilino-8-naphthalenesulfonate, circular dichroism measurements, and electron microscopy [8].
• Finally, by both activity and fluorescence measurements we have found that 1-anilino-8-naphthalenesulfonate has access to the active site of mini-Lox but not to that of intact Lox-1 [9].
• Affinity capillary electrophoresis experiments showed increased specific interactions of the nonnative beta(2)-microglobulin conformation with the dyes 8-anilino-1-naphthalene sulfonic acid and Congo red [10].

Chemical compound and disease context of Phenylperi acid

• The urea-induced unfolding at pH 7.5 of Escherichia coli phosphoenolpyruvate (P-pyruvate) carboxykinase was studied by monitoring the enzyme activity, intrinsic protein fluorescence, circular dichroism spectra, and 1-anilino-8-naphthalenesulfonate binding [11].
• Pseudomonas aeruginosa, isolated from soil near tannery effluent was able to degrade 8-anilino-1-naphthalenesulfonic acid (ANSA), a sulfonated aromatic amine [5].

Biological context of Phenylperi acid

• Besides binding vinblastine, tubulin was shown to bind vincristine with identical free energy and stoichiometry and to have a single binding site for 8-anilino-1-naphthalene sulfonic acid per tubulin dimer, which is independent of those for vinblastine [12].
• Analysis of the time courses of 32Pi esterification and decays of the pH difference and membrane potential, followed using 9-aminoacridine and 8-anilinonaphthalene-1-sulfonate, respectively, as probes, showed a relationship between delta-micronH+ and the rate of ATP synthesis [13].
• Measurements of 8-anilino-1-naphthalenesulfonic acid fluorescence in the particles indicated that glucagon treatment resulted in a stimulation of energization supported by succinate respiration or ATP hydrolysis [14].
• At intermediate concentrations (14.3 +/- 4.8 nmol/mg of membrane protein), reserpine abolishes the ATP-dependent enhancement of 8-anilinonaphthalene-1-sulfonate fluorescence without affecting the ATP-dependent membrane potential [15].
• Fluorescence energy transfer experiments using 1-anilino-8-naphthalenesulfonate indicate that at least one of the three tryptophan residues in the A form is accessible to water [16].

Anatomical context of Phenylperi acid

• Interaction of nucleotides and cations with the (Ca2+, Mg2+)-ATPase of sarcoplasmic reticulum as determined by fluorescence changes of bound 1-anilino-8-naphthalenesulfonate [17].
• The presence of analogue phospholipids also altered the interaction of 8-anilino-1-naphthalene sulfonic acid with LM cell membranes [18].
• Effect of a phase transition on the binding of 1-anilino-8-naphthalenesulfonate to phospholipid membranes [19].
• Effect of 1-anilino-8-naphthalene sulfonate (ANS) on transferrin and iron uptake by reticulocytes [20].
• Membrane permeability transition promoted by phosphate enhances 1-anilino-8-naphthalene sulfonate fluorescence in calcium-loaded liver mitochondria [21].

Associations of Phenylperi acid with other chemical compounds

• The central role of hydrophobic interactions in dimer formation has been revealed by the 30% increase of exposure of the tryptophan cluster to quenchers upon dissociation of RT and the binding of 4 equiv of 1-anilino-8-naphthalenesulfonate to the dissociated enzymes [22].
• The binding characteristics of several amine drugs with dispersed phospholipids (phosphatidylcholine, phosphatidylserine, and phosphatidylglycerol) have been studied using the fluorometric method and 1-anilino-8-naphthalene sulfonate and 1,6 diphenyl-1,3,5-hexatriene as fluorescence probes [23].
• The fluorescence of four dyes (8-anilino-1-naphthalenesulfonic acid, merocyanine 540, 3,3'-dipropyl-thiocarbocyanine, and bis[1,3-dibutylbarbituric acid-(5)]-pentamethine oxonol) was found to respond appropriately to changes in an apparent K+ diffusion potential [24].
• The binding of thyroxine (T4) and 8-anilino-1-naphthalenesulfonic acid (ANS) to human serum prealbumin was measured by equilibrium dialysis at pH 7.4 in 0.05 M phosphate-0.10 M NaCl at 25 degrees [25].
• Analysis of thyroid hormone binding to human serum prealbumin by 8-anilinonaphthalene-1-sulfonate fluorescence [26].

Gene context of Phenylperi acid

• Substrate binding to phosphoglycerate kinase monitored by 1-anilino-8-naphthalenesulfonate [27].
• We followed the steps preceding IAPP insolubilization and amyloid formation in vitro using a variety of biochemical methods, including a filtration assay, far and near-UV circular dichroism (CD) spectropolarimetry, 1-anilino-8-naphthalenesulfonic acid (ANS) binding, and atomic force (AFM) and electron (EM) microscopy [28].
• ANS (8-anilinonaphthalene-1-sulfonic acid) binding and affinity chromatography on a hydrophobic column suggested that both the Ca(2+)-free and Ca(2+)-loaded form of calbindin D(28k) have exposed hydrophobic surfaces [29].
• Consistent with this last idea, clusterin has been shown to bind to a variety of molecules with high affinity including lipids, peptides, and proteins and the hydrophobic probe 1-anilino-8-naphthalenesulfonate (ANS) [30].
• Likewise, removal of EF-hands 3 and 4 distorted the ability of KChIP1 to bind with Kv4.2 N-terminal fragment (KvN) as well as fluorescent probe 8-anilinonaphthalene-1-sulfonate (ANS) [31].

Analytical, diagnostic and therapeutic context of Phenylperi acid

• Circular dichroism studies show structural changes in the chimeric proteins. alphaBNAC binds more 8-anilinonaphthalene-1-sulfonic acid than the alphaANBC and the wild-type proteins, indicating increased accessible hydrophobic regions [32].
• Fluorescence titration with 8-anilinonaphthalene-1-sulfonate revealed a strong and a weak binding site for BrAcT4 (K1 = 1 X 10(8) M-1; K2 = 1 X 10(6) M-1) [33].
• Data from 8-anilinonaphthalene-1-sulfonic acid fluorescence, size-exclusion chromatography, and heteronuclear NMR strongly suggest the presence of a folding intermediate at 1.5 m GdnHCl for SCM protein [34].
• We report a solid-phase iodine- 125 radioimmunoassay for serum cortisol in which the interfering binding proteins are inactivated by a combination of reaction pH and 8-anilino-1-naphthalenesulfonic acid [35].
• DTT-IL-6 appears to form a partially unfolded and highly aggregated conformation under all conditions studied, as showed by a high propensity to self-associate (demonstrated using a biosensor employing surface plasmon resonance), and an increased ability to bind the hydrophobic probe 8-anilino-1-naphthalenesulfonic acid [36].

References