Determination of the critical micelle concentration of surfactants using the fluorescent probe N-phenyl-1-naphthylamine

Brito, Rui M. M.; Vaz, Winchil L.C.

doi:10.1016/0003-2697(86)90406-9

Cited by 214 publications

(93 citation statements)

References 9 publications

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“…www.bjournal.com.br zwitterionic homologues, Zwit 3-14 and Zwit 3-16, with equivalent acyl chains: CMC = 121 and 11.3 µM, respectively, in water (19) and 140 and 14 µM, respectively, in 0.1-0.2 M NaCl (20).…”

Section: Resultsmentioning

confidence: 99%

Solubilization of human erythrocyte membranes by ASB detergents

Domingues

Malheiros

Paula

2008

Braz J Med Biol Res

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Understanding the membrane solubilization process and finding effective solubilizing agents are crucial challenges in biochemical research. Here we report results on the interaction of the novel linear alkylamido propyl dimethyl amino propanosulfonate detergents, ASB-14 and ASB-16, with human erythrocyte membranes. An estimation of the critical micelle concentration of these zwitterionic detergents (ASB-14 = 100 µM and ASB-16 = 10 µM) was obtained using electron paramagnetic resonance. The amount of proteins and cholesterol solubilized from erythrocytes by these detergents was then determined. The hemolytic activities of the ASB detergents were assayed and the detergent/lipid molar ratios for the onset of hemolysis (R e sat ) and total lysis (R e sol ) were calculated, allowing the determination of the membrane binding constants (K b ). ASB-14 presented lower membrane affinity (K b = 7050 M -1 ) than ASB-16 (K b = 15610 M -1 ). The amount of proteins and cholesterol solubilized by both ASB detergents was higher while R e sat values (0.22 and 0.08 detergent/lipid for ASB-14 and ASB-16, respectively) were smaller than those observed with the classic detergents CHAPS and Triton X-100. These results reveal that, besides their well-known use as membrane protein solubilizers to enhance the resolution of two dimensional electrophoresis/ mass spectrometry, ASB-14 and ASB-16 are strong hemolytic agents. We propose that the physicochemical properties of ASB detergents determine their membrane disruption efficiency and can help to explain the improvement in the solubilization of membrane proteins, as reported in the literature.

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Section: Resultsmentioning

confidence: 99%

Solubilization of human erythrocyte membranes by ASB detergents

Domingues

Malheiros

Paula

2008

Braz J Med Biol Res

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“…Reaction products were subjected to ultracentrifugation, and aliquots of the resultant supernatants and resuspended pellets were assayed for protein and [ Buffer at varying concentrations (1 M to 10 mM) were incubated for 1 h (at 37°C or room temperature) in the presence of 10 M N-phenyl-1-naphthylamine, after which fluorescence intensity was read directly in a PTI fluorimeter ( ex ϭ 346 nm, em ϭ 420 nm, 1 nm bandwidth, 800 V, gain 12.5, and slit 16) jacketed at 37°C. When present, htau40 was maintained at 4 M. CMCs were estimated from abscissa intercepts after least squares linear regression as described previously (24) and expressed as CMC Ϯ S.E. of the estimate.…”

Section: Methodsmentioning

confidence: 99%

Anionic Micelles and Vesicles Induce Tau Fibrillization in Vitro

Chirita

Necula

Kuret

2003

Journal of Biological Chemistry

220

255

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Alzheimer's disease is defined in part by the intraneuronal accumulation of filaments comprised of the microtubule-associated protein tau. In vitro, fibrillization of recombinant tau can be induced by treatment with various agents, including phosphotransferases, polyanionic compounds, and fatty acids. Here we characterize the structural features required for the fatty acid class of tau fibrillization inducer using recombinant fulllength tau protein, arachidonic acid, and a series of straight chain anionic, cationic, and nonionic detergents. Induction of measurable tau fibrillization required an alkyl chain length of at least 12 carbons and a negative charge consisting of carboxylate, sulfonate, or sulfate moieties. All detergents and fatty acids were micellar at active concentrations, due to a profound, taudependent depression of their critical micelle concentrations. Anionic surfaces larger than detergent micelles, such as those supplied by phosphatidylserine vesicles, also induced tau fibrillization with resultant filaments originating from their surface. These data suggest that anionic surfaces presented as micelles or vesicles can serve to nucleate tau fibrillization, that this mechanism underlies the activity of fatty acid inducers, and that anionic membranes may serve this function in vivo.

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“…When present, ␣-synuclein was maintained at 4 M for the positively charged detergents and at 15 M for the anionic detergents and arachidonic acid. CMCs were estimated from abscissa intercepts after least squares linear regression as described previously (46) and were expressed as CMC Ϯ S.E. of the estimate.…”

Section: Materials-arachidonicmentioning

confidence: 99%

Rapid Anionic Micelle-mediated α-Synuclein Fibrillization in Vitro

Necula¹,

Chirita²,

Kuret

2003

Journal of Biological Chemistry

200

206

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Parkinson's disease is characterized by the aggregation of ␣-synuclein into filamentous forms within affected neurons of the basal ganglia. Fibrillization of purified recombinant ␣-synuclein is inefficient in vitro but can be enhanced by the addition of various agents including glycosaminoglycans and polycations. Here we report that fatty acids and structurally related anionic detergents greatly accelerate fibrillization of recombinant ␣-synuclein at low micromolar concentrations with lag times as short as 11 min and apparent first order growth rate constants as fast as 10.4 h ؊1 . All detergents and fatty acids were micellar at active concentrations because of an ␣-synuclein-dependent depression of their critical micelle concentrations. Other anionic surfaces, such as those supplied by anionic phospholipid vesicles, also induced ␣-synuclein fibrillization, with resultant filaments originating from their surface. These data suggest that anionic surfaces presented as micelles or vesicles can serve to nucleate ␣-synuclein fibrillization, that this mechanism underlies the inducer activity of anionic surfactants, and that anionic membranes may serve this function in vivo.

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Determination of the critical micelle concentration of surfactants using the fluorescent probe N-phenyl-1-naphthylamine

Cited by 214 publications

References 9 publications

Solubilization of human erythrocyte membranes by ASB detergents

Solubilization of human erythrocyte membranes by ASB detergents

Anionic Micelles and Vesicles Induce Tau Fibrillization in Vitro

Rapid Anionic Micelle-mediated α-Synuclein Fibrillization in Vitro

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