Anilinonaphthalene sulfonate as a probe of membrane composition and function

Slavík, Jan

doi:10.1016/0304-4157(82)90012-0

Cited by 517 publications

(228 citation statements)

References 226 publications

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“…By virtue of its sensitivity, selectivity, and large temporal range, fluorescence spectroscopy has become one of the most revealing windows on biomolecular dynamics (Slavik, 1982;Lakowicz, 2000). Our aim was to elaborate a new fluorescent-based method for use in immunologic-based diagnostics of gastrointestinal cancer patients.…”

Section: Introductionmentioning

confidence: 99%

Altered plasma albumin characteristics and lymphocyte populations in gastrointestinal cancer patients: Detection using modified fluorescence responses

Kalnina

Kirilova

Klimkane

et al. 2009

Journal of Immunotoxicology

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Section: Introductionmentioning

confidence: 99%

Altered plasma albumin characteristics and lymphocyte populations in gastrointestinal cancer patients: Detection using modified fluorescence responses

Kalnina

Kirilova

Klimkane

et al. 2009

Journal of Immunotoxicology

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“…In membranes com- posed of a mixture of different lipids, most 1-anilino-8-naphthalenesulphonate molecules are bound in lecithin-sphingomyelin pockets, or to a much lesser extent in the shallow binding sites associated with the presence of chplesterol, although cholesterol alone does not bind l^anilino-8-napbthaleriesulphonate at all. Since lecithin and sphingomyelin heads bind l-anilino-8-naphthalenesulphonate most avidly, the first mentioned type of binding will essentially pre--dorpinate (4,19). An increased cholesterol: lecithin molar ratio leads to the other, quite different type of l -anilino-8-naphthalenesulphonate binding, where l-amlino-8-naphthaleüesulphonate molecules are located in cholesterol-legithin pockets, which are much morfc expösed to extrinsic water.…”

Section: Discussionmentioning

confidence: 99%

“…Although certain aspects of l-anilino-8-naphthalenesulphonate fluorescence remain to be evaluated, numerous physical parameters of l-anilino-8-naphthalenesulphonate fluorescence have already been thoroughly explored. It was therefore possible to develop an adequate methodological approach to the reliable study of l-anilino-8-naphthalenesulphonate fluorescence alterations (4). Showing negligible interference with membranes and possessing convenient adsorption characteristics, l-anilino-8-naphthalenesulphonate remains the fluorescence probe of choice for numerous in vivo and in vitro experiments.…”

Section: Troductionmentioning

confidence: 99%

1-Anilino-8-naphthalenesulphonate Binding Parameters in Red Cell Membranes. Does Diabetes Mellitus Affect Cell Membrane Dynamics?

Watała

Jóźwiak²

1989

Clinical Chemistry and Laboratory Medicine

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Summary:In this study we report the use of l-anilino-8-naphthalenesulphonate äs a fluorescence probe to investigate the properties of plasma membranes derived from normal and diabetic red blood cells.The binding of l-anilino-8-naphthalenesulphonate to diabetes-affected erythrocyte membranes, äs compared with controls, was measured by means of fluorescence polarization and fluorescence titration techniques.These measurements demonstrated anomalous l-anilino-^S-naphthalenesulphonate binding to pathological red cell membranes. The amount of l-anilino-8-naphthalenesulphonate bound to diabetic erythrocyte membranes was greater than that of controls. This fluorometric study indicated that the outer monolayer binding of l-anilino-8-naphthalenesulphonate was markedly augmented in the erythrocyte membranes of diabetic patients. Significant correlations were found between l-anilino-8-naphthalenesulphonate binding parameters and membrane lipid composition. The correlation between these binding parameters and non-enzymatic protein glycation was poor or moderate.Though the fluorescence intensity and emission maximum were quite similar in both groups investigated, binding studies reveäled that there were approximately 1.2 times the number of l-anilino-8-naphthalenesulphonate binding sites and a 33% increase in the K O value in diabetic membranes, suggesting significant differences in the environment of the l-anilino-8-naphthalenesulphonate binding sites in these two groups of patients.The results presented in this report indicate that (a) l-aniliüo-8-naphthalenesulphonate is a sensitive probe of membrane architecture alterations, and can be used to elucidate the perturbating effects of sterols in membrane Systems, and (b) that significant differences in membrane dynamics exist between normal and diabetic red cell membranes.The possibility that the increase in bound dye in diabetics was caused by enhanced lateral compressibility, or deiisity flüctuations, of whether it was due to additional binding sites at the boundary of heterogeneous lipid chisters is discussed. troductiono f fluorescence spectroscopy has been The revival of interest in fluorescence probes in recent used to probe many parameters of membrane strucyears has resulted in numerous studies dealing with ture using a variety of extrinsic probe molecules (2, thepertinehcepfselectedflüorophoresformonitoring 3), and several cheinicals have been especially dechanges of membrane structure and dynamics (l, 2), signed for this purpose. Amongst them, l-anilino-8-

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“…Looking in more detail into the HlyAcalcium system, the above authors observed that, even in the absence of lipid bilayers, Ca 2+ binding had significant effects on α-hemolysin. In particular, binding to Ca 2+ exposes new hydrophobic residues on the protein surface, as indicated by the increased binding of the fluorescent probe aniline naphtholsulfonate (ANS), that is known to bind with high affinity hydrophobic molecules or molecule regions (85,86), and by the increase in size of the protein aggregates that α-hemolysin forms in aqueous media.…”

Section: More On the Role Of Divalent Cationsmentioning

confidence: 99%

E. coli <FONT FACE=Symbol>a</FONT>-hemolysin: a membrane-active protein toxin

Goñi

Ostolaza

1998

Braz J Med Biol Res

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Alpha-Hemolysin is synthesized as a 1024-amino acid polypeptide, then intracellularly activated by specific fatty acylation. A second activation step takes place in the extracellular medium through binding of Ca2+ ions. Even in the absence of fatty acids and Ca2+ HlyA is an amphipathic protein, with a tendency to self-aggregation. However, Ca2+-binding appears to expose hydrophobic patches on the protein surface, facilitating both self-aggregation and irreversible insertion into membranes. The protein may somehow bind membranes in the absence of divalent cations, but only when Ca2+ (or Sr2+, or Ba2+) is bound to the toxin in aqueous suspensions, i.e., prior to its interaction with bilayers, can a-hemolysin bind irreversibly model or cell membranes in such a way that the integrity of the membrane barrier is lost, and cell or vesicle leakage ensues. Leakage is not due to the formation of proteinaceous pores, but rather to the transient disruption of the bilayer, due to the protein insertion into the outer membrane monolayer, and subsequent perturbations in the bilayer lateral tension. Protein or glycoprotein receptors for a-hemolysin may exist on the cell surface, but the toxin is also active on pure lipid bilayers

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Anilinonaphthalene sulfonate as a probe of membrane composition and function

Cited by 517 publications

References 226 publications

Altered plasma albumin characteristics and lymphocyte populations in gastrointestinal cancer patients: Detection using modified fluorescence responses

Altered plasma albumin characteristics and lymphocyte populations in gastrointestinal cancer patients: Detection using modified fluorescence responses

1-Anilino-8-naphthalenesulphonate Binding Parameters in Red Cell Membranes. Does Diabetes Mellitus Affect Cell Membrane Dynamics?

E. coli <FONT FACE=Symbol>a</FONT>-hemolysin: a membrane-active protein toxin

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