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8-Anilinonaphthalene-1-sulphonate interaction with whole and disrupted mitochondria: a re-evaluation of the use of double-reciprocal plots in the derivation of binding parameters for fluorescent probes binding to mitochondrial membranes.

ABSTRACT: It is shown that 8-anilinonaphthalene-1-sulphonate is a permeant anion of whole mitochondrial membranes. It is also shown experimentally and algebraically that plots of reciprocal fluorescence against reciprocal membrane concentration, at a fixed 8-anilino-naphthalene-1-sulphonate concentration, are straight lines even when more than one binding site is involved.

SUBMITTER: Gains N

PROVIDER: S-EPMC1165518 | biostudies-other | 1975 Apr

REPOSITORIES: biostudies-other

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1-Anilinonaphthalene-8-sulphonate, a fluorescent conformational probe for glutamate dehydrogenase.

Project description:1. The interaction of 1-anilinonaphthalene-8-sulphonate with ox liver glutamate dehydrogenase was examined. 2. The fluorescence of the dye is enhanced 100-fold on binding. 3. A further enhancement is observed when NADH and GTP are added to the enzyme. 4. By using this property of the dye to measure conformational equilibria in the enzyme the effects of coenzyme, inhibitors, enzyme concentration, ionic strength and pH on the allosteric transitions were studied. 5. GTP and NADH interact with the enzyme in a heterotropic manner. 6. The rate of the structural transition brought about by GTP and NADH is biphasic with half-lives of 34 and 200msec. 7. The relation of these observations to regulatory mechanisms is discussed.

| S-EPMC1184868 | biostudies-other

Iron-dependent binding of 8-anilinonaphthalene-1-sulphonate by both lactoferrin and transferrin.

Project description:Fluorescence of 8-anilinonaphthalene-1-sulphonate is enhanced by both lactoferrin and transferrin. The enhancement is relatively low between pH 4 and 8, and high at below pH 4. At physiological pH the fluorescence enhancement is higher with the iron-deprived than with the iron-saturated proteins. Binding of iron by lactoferrin is associated with lowering affinity for the dye.

| S-EPMC1163837 | biostudies-other

A role for phospholipids in the binding and metabolism of drugs by hepatic microsomes. Use of the fluorescent hydrophobic probe 1-anilinonaphthalene-8-sulphonate.

Project description:1. The pretreatment of rat liver microsomes with phospholipase C or D decreased the N-demethylation of (+)-benzphetamine. The hydroxylation of aniline was essentially unchanged by pretreatment of microsomes with phospholipase C. 2. Some components of the microsomal mixed-function oxidase system were impaired by phospholipases. 3. The fluorescence of 1-anilinonaphthalene-8-sulphonate (ANS) was greatly enhanced by microsomes. Phospholipase C or D markedly decreased ANS-microsome fluorescence. Quantum yield of ANS-microsome fluorescence appeared to be related directly to phospholipid content of microsomes. 4. Most of the drugs studied enhanced ANS-microsome fluorescence. Warfarin, however, displaced ANS fluorescence competitively from microsomes. The latter effect was postulated as being due to warfarin competing with ANS for the cationic site on microsomal phosphatidylcholine. 5. ANS fluorescence was also increased by the presence of phospholipid micelles. The fluorescence of ANS-phosphatidylcholine micelles was modified by warfarin and (+)-benzphetamine in a manner similar to that observed with microsomes. Warfarin decrease of fluorescence was absent when ANS was bound to phosphatidic acid, which lacks a cationic site. 6. Trypsin pretreatment of microsomes did not modify ANS-microsome fluorescence, including drug-induced changes. 7. It was postulated that phospholipids have a permissive role in the metabolism of most drugs by hepatic microsomes and that the ANS probe might reflect interactions of compounds with microsomal membrane phospholipids.

| S-EPMC1176993 | biostudies-other

The binding of 8-anilinonaphthalene-1-sulphonate to cytoplasmic aspartate aminotransferase from pig heart.

Project description:Anilinonaphthalenesulphonate binds to cytoplasmic aspartate aminotransferase with high affinity (Kd about 10 muM) and with a stoicheiometry of one molecule per dimer. It is not displaced by aliphatic or aromatic dicarboxylate substrate analogues. The enzyme is believed to be a symmetrical dimer with identical subunits; it can evidently function asymmetrically in binding anilinonaphthalenesulphonate.

| S-EPMC1165195 | biostudies-other

Structure of the human-heart fatty-acid-binding protein 3 in complex with the fluorescent probe 1-anilinonaphthalene-8-sulphonic acid.

Project description:Heart-type fatty-acid-binding protein (FABP3), which is a cytosolic protein abundantly found in cardiomyocytes, plays a role in trafficking fatty acids throughout cellular compartments by reversibly binding intracellular fatty acids with relatively high affinity. The fluorescent probe 1-anilinonaphthalene-8-sulfonate (ANS) is extensively utilized for examining the interaction of ligands with fatty-acid-binding proteins. The X-ray structure of FABP3 was determined in the presence of ANS and revealed the detailed ANS-binding mechanism. Furthermore, four water molecules were clearly identified in the binding cavity. Through these water molecules, the bound ANS molecule forms indirect hydrogen-bond interactions with FABP3. The adipocyte-type fatty-acid-binding protein (FABP4) exhibits 67% sequence identity with FABP3 and its crystal structure is almost the same as that of FABP3. However, FABP4 can bind with a higher affinity to ANS than FABP3. To understand the difference in their ligand specificities, a structural comparison was performed between FABP3-ANS and FABP4-ANS complexes. The result revealed that the orientation of ANS binding to FABP3 is completely opposite to that of ANS binding to FABP4, and the substitution of valine in FABP4 to leucine in FABP3 may result in greater steric hindrance between the side-chain of Leu115 and the aniline ring of ANS.

| S-EPMC3795557 | biostudies-literature

8-Styryl-substituted coralyne derivatives as DNA binding fluorescent probes.

Project description:Six new 8-styryl-substituted coralyne derivatives 4a-f were synthesized from coralyne (2) by a base catalysed Knoevenagel type reaction. It was shown by photometric and fluorimetric titrations of double stranded and quadruplex DNA to 4b-d as well as by fluorimetric DNA denaturation experiments that these ligands bind to DNA with different binding modes at varying ligand-DNA ratios (LDR). Specifically, the addition of DNA caused initially a hypochromic effect in absorbance and, at a particular LDR, the development of a new red shifted absorption band with a hyperchromic effect. Furthermore, 4b-d induced a significant and selective stabilization of quadruplex DNA towards unfolding (ΔTm = 31.6-32.9 °C at LDR = 5), which is even more pronounced as compared to the parent compound coralyne (2). Most notably, the addition of DNA to the dimethylamino-substituted derivative 4b leads to a new, strongly red-shifted emission band at 695 nm. Hence, this derivative is a fluorescent probe that changes its fluorescence colour from green to red in the presence of DNA and even allows the fluorimetric analysis of living cells by staining of the nucleoli.

| S-EPMC5361113 | biostudies-literature

Sigmoid curves, non-linear double-reciprocal plots and allosterism.

Project description:1. The theory of plane curves was applied to the graphical methods used in enzyme kinetics and a mathematical analysis of the possible graph shapes is given. 2. The belief that allosterism can be inferred from steady-state data alone is subjected to criticism and the mathematical significance of sigmoid curves and non-linear double-reciprocal plots is explored. 3. It is suggested that the usual methods of interpreting steady-state kinetic data are often based on over-restrictive assumptions which prevent maximum utilization of the available data. 4. Methods for obtaining the degree of the rate equation from graph shapes obtained directly from initial-rate measurements and from replots of asymptotic behaviour as chi approach the level 0 and chi approach the level infinity are discussed. 5. Detailed proofs of the theorems given in the text have been deposited as Supplementary Publication SUP 50049 (10 pages) at the British Library (Lending Division), Boston Spa, West Yorkshire LS23 7BQ, U.K., from whom copies can be obtained on the terms indicated in Biochem. J. (1975), 145, 5.

| S-EPMC1165625 | biostudies-other

Fluorescent probes of the isoxazole-dihydropyridine scaffold: MDR-1 binding and homology model.

Project description:Isoxazole-1,4-dihydropyridines (IDHPs) were tethered to fluorescent moieties using double activation via a lanthanide assisted Weinreb amidation. IDHP-fluorophore conjugate 3c exhibits the highest binding to date for IDHPs at the multidrug-resistance transporter (MDR-1), and IDHP-fluorophore conjugates 3c and 7 distribute selectively in SH-SY5Y cells. A homology model for IDHP binding at MDR-1 is presented which represents our current working hypothesis.

| S-EPMC3987963 | biostudies-literature

Genetically encoded fluorescent redox probes.

Project description:Redox processes are involved in almost every cell of the body as a consequence of aerobic life. In the past decades, redox biology has been increasingly recognized as one of the key themes in cell signaling. The progress has been accelerated by development of fluorescent probes that can monitor redox conditions and dynamics in cells and cell compartments. This short paper focuses on fluorescent redox probes that are genetically encoded, and discusses their properties, molecular mechanism, advantages and pitfalls. Our recent work on reaction-based encoded probes that are responsive to particular redox signaling molecules is also reviewed. Future challenges and directions are also commented.

| S-EPMC3871076 | biostudies-literature

Competitive binding of fatty acids and the fluorescent probe 1-8-anilinonaphthalene sulfonate to bovine beta-lactoglobulin.

Project description:The use of spectroscopy in the study of fatty acids binding to bovine beta-lactoglobulin (BLG) appears to be a difficult task, as these acid compounds, assumed as the protein natural ligands, do not exhibit favorable optical response such as, for example, absorption or fluorescence. Therefore, the BLG fatty-acid equilibrium has been tackled by exploiting the competition between fatty acids and ANS, a widely used fluorescent hydrophobic probe, whose binding sites on the protein have been characterized recently. Two lifetime decays of the ANS-BLG complex have been found; the longer one has been attributed to the internal binding site and the shorter one to the external site. At increasing fatty acids concentration, the fractional weight associated with ANS bound to the internal site drops, in agreement with a model describing the competition of the dye with fatty acids, whereas the external site occupancy appears to be unaffected by the fatty acids binding to BLG. This model is supported by docking studies. An estimate of the acid-binding affinities for BLG has been obtained by implementing the fitting of the bound ANS intensities with a competitive binding model. A relevant dependence has been found upon the solution pH, in the range from 6 to 8, which correlates with the calyx accessibility modulated by the conformation of the EF loop. Fatty acids with longer aliphatic chains (palmitate and laurate) are found to display larger affinities for the protein and the interaction free energy nicely correlates with the number of contacts inside the protein calyx, in agreement with docking simulations.

| S-EPMC2323946 | biostudies-other

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