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PubMed1981

Phosphorescence studies of the interaction of myelin basic protein with phosphatidylserine vesicles.

Phosphorescence from the lone tryptophan residue has been studied to monitor the interaction of myelin basic protein with phosphatidylserine vesicles. Spectral shifts in the phosphorescence of the protein in a glycerol-buffer (70:30 w/w) solvent at low temperature are consistent with fluorescence data obtained under ambient conditions, indicating that the tryptophan side chain is exposed to the solvent in the free protein but is buried on interaction with a lipid bilayer. Measurements of the phosphorescence intensity and lifetime as a function of temperature reveal a marked protection of the tryptophan to thermally induced quenching in the presence of phosphatidylserine vesicles. Steady-state anisotropy measurements on the tryptophan phosphorescence were used to follow the slow motions of the protein associated with the synthetic bilayer. The observations that the rotational correlation time for the membrane-associated protein is 4 X 10(3) times that anticipated for a molecule the size of basic protein reflects its partial intrinsic character in the membrane.

Animals↗

PubMed1997

Time-resolved protein phosphorescence in the stopped-flow: denaturation of horse liver alcohol dehydrogenase by urea and guanidine hydrochloride.

This study reports the implementation of room temperature protein phosphorescence in the stopped-flow technique. Time-resolved Trp phosphorescence can now be detected following rapid mixing of protein solutions with a time resolution of 10 ms and a sensitivity in terms of chromophore concentration down to 0.1 microM. Calibration tests with monomeric and multimeric proteins proved that in all cases the delayed emission is not affected by artefacts that could arise from either enrichment of trace impurities along the flow lines or deformation of the macromolecules by the shear stress of laminar flow. To illustrate the potential of Trp phosphorescence in the stopped-flow to detect the time evolution of protein conformation the interaction of urea and guanidine hydrochloride (GdnHCl) with the native structure of horse liver alcohol dehydrogenase (LADH) has been re-examined under conditions of rapid denaturation. Remarkable differences in the action of the two denaturing agents has been confirmed by the phosphorescence lifetime (tauP) of the internal Trp residue (W314). Whereas in urea, up to 8 M, tauP is not minimally perturbed, in GdnHCl it decreases sharply and progressively from 800 ms down to 23 ms in 6 M solutions. Such reduction of tauP implies that in the region of W314 the polypeptide structure has become highly loose and flexible prior to the major unfolding transition. Therefore, denaturation of LADH in GdnHCl, as opposed to urea, proceeds from a partly unfolded intermediate conformation of the protein. Other characteristics of this intermediate state are a partial loss of tertiary structure, as revealed by the circular dichroism of the aromatics, and an almost complete inhibition of the catalytic activity. Control experiments with equimolar NaCl demonstrate that tauP, the tertiary structure and the catalytic activity are affected to a much smaller extent and that, therefore, salt effects do not account for the difference between urea and GdnHCl. Finally, measurements of the unfolding reaction emphazise that the kinetics of LADH denaturation are heterogeneous with both denaturing agents. From the constancy of tauP during the course of the reaction it is concluded that the multiphasic behavior is a manifestation of multiple unfolding pathways owing to a plurality of stable LADH conformations.

Alcohol Dehydrogenase↗

PubMed2000

Hydrogen exchange at the core of Escherichia coli alkaline phosphatase studied by room-temperature tryptophan phosphorescence.

The room-temperature tryptophan (Trp) phosphorescence lifetime is sensitive to details of the local environment and has been shown to increase significantly in some proteins following H-D exchange. Careful analysis of the phosphorescence lifetime distribution of Trp 109 in Escherichia coli alkaline phosphatase (AP) in solution as a function of time during the H-D exchange shows that this process corresponds to a two-state reaction resulting from the deuteration of a single, specific hydrogen in the core of the protein. The absence of a pH dependence of the exchange rate suggests that the exchange is not an EX2 process, and therefore, a certain degree of unfolding is required for exchange to occur. This discovery opens up the use of phosphorescence-detected hydrogen exchange as a sensitive tool for monitoring the local susceptibility and activation energy for exchange in proteins having a phosphorescent Trp and, for example, for studying the effects of local mutations upon that susceptibility.

Alkaline Phosphatase↗

PubMed2002

1,8-Naphthalimides in phosphorescent organic LEDs: the interplay between dopant, exciplex, and host emission.

Four different 1,8-naphthalimide derivatives were examined in phosphorescent organic light emitting diodes (OLEDs), i.e., 1,8-naphthalimide, N-phenyl-1,8-naphthalimide, N-2,6-dibromophenyl-1,8-naphthalimide (niBr), and bis-N,N-1,8-naphthalimide. Photoluminescence from all four naphthalimides have violet-blue fluorescence and phosphorescent bands between 550 and 650 nm (visible at 77 K). While all four compounds gave good glassy films when doped with a phosphorescent dopant, only the niBr films remained glassy for extended periods. OLED studies focused on niBr, with two different architectures. One OLED structure (type 1) had the niBr layer as a doped luminescent layer and an undoped niBr layer to act as a hole-blocking layer. The alternate structure (type 2) utilizes a doped CBP layer as the luminescent layer and the niBr layer is used as a hole-blocking layer only (CBP = 4,4'-N,N'-dicarbazolylbiphenyl). Type 1 and 2 OLEDs were prepared with green, yellow, and red emissive phosphorescent dopants (Irppy, btIr, and btpIr, respectively). The dopants were organometallic Ir complexes, previously shown to give highly efficient OLEDs. Of the three dopants, the btpIr-based OLEDs showed the best device performance in both structures (peak efficiencies for type 2: 3.2% and 2.3 lum/W at 6.3 V; type 1: 1.7% and 1.3 lm/W at 6.1 V). The green and yellow dopants gave very similar performance in both type 1 and 2 devices (peak efficiencies are 0.2-0.3%), which were significantly poorer than the btpIr-based OLEDs. The emission spectrum of the btIr- and btpIr-based devices (type 1 and 2) are the same as the solution photoluminescence spectrum of the dopant alone, while the Irppy device gives a broad red emission line (lambda(max) = 640 nm). The red Irppy.niBr emission line is assigned to an Irppy.niBr exciplex. The type 2 Irppy-based device gave a voltage-dependent spectrum, with the red emission observed at low bias (4-8 V), switching over to strong green emission as the bias was raised. All other devices showed bias-independent spectra. Estimates of HOMO, LUMO, and excited-state energies (dopant, niBr, and exciplex) were used to explain the observed spectral properties of these devices. btpIr-based devices emit efficiently from isolated dopant states (external efficiencies = 3.2 %, 2.3 lum/W). Irppy-based devices emit only from exciplex states, with low efficiency (external efficiency = 0.3%). btIr.niBr films have very similar energies for the dopant, exciplex, and niBr triplet states, such that relaxation can go through any of these states, leading to low device efficiency (external efficiency = 0.4%). High device efficiency is achieved only when dopant emission is the dominant pathway for relaxation, since exciplex and niBr triplet states give either weak or no electroluminescence.

Journal Article↗

PubMed2006

Dark-field oxidative addition-based chemosensing: new bis-cyclometalated PtII complexes and phosphorescent detection of cyanogen halides.

Heavy metal complexes that are phosphorescent at room temperature are becoming increasingly important in materials chemistry, principally due to their use in phosphorescent organic light-emitting devices (OLEDs). Their use in optical sensory schemes, however, has not been heavily explored. Homoleptic bis-cyclometalated Pt(II) complexes are known to undergo oxidative addition with appropriate electrophiles (principally alkyl halides) by either thermal or photochemical activation. We have applied this general reaction scheme to the development of a phosphorescence-based sensing system for cyanogen halides. To carry out structure-property relationship studies, a series of previously unreported Pt(II) complexes was prepared. Most of the complexes (excluding those that incorporated substituents on the ligands that forced steric crowding in the square plane) were strongly orange-red phosphorescent (Phi = 0.2-0.3) in a room-temperature oxygen-free solution. These sterically demanding ligands also accelerated the addition of cyanogen bromide to these complexes but slowed the addition of methyl iodide, indicating that the oxidative addition mechanisms for these two electrophiles is different. The lack of solvent-polarity effect on the addition of BrCN suggests a radical mechanism. Oxidative addition of BrCN to the metal complexes in solution or dispersed in poly(methyl methacrylate) gave blue-shifted emissive Pt(IV) complexes. The blue-shifted products give a dark-field sensing scheme that is in sharp contrast to energy transfer-based sensing schemes, which have limited signal-to-noise because of the presence of lower-energy vibronic bands of the energy donor that can overlap with the emission of the acceptor.

Crystallography, X-Ray↗

PubMed2002

Determination of the pesticide napropamide in soil, pepper, and tomato by micelle-stabilized room-temperature phosphorescence.

A selective and sensitive method for determining napropamide by room-temperature phosphorescence in SDS micelles is proposed and applied to the determination of this substance in a technical formulation and in spiked soil, pepper, and tomato samples. The use of phosphorescence enhancers such as sodium dodecyl sulfate (micellar agent), thallium (I) nitrate (external heavy atom), and sodium sulfite (deoxygenation agent) was studied and optimized to obtain maximum sensitivity. The determination was performed in 66 mM SDS, 30 mM thallium (I) nitrate, and 8 mM sodium sulfite. Taking into account both maximum phosphorescence intensity and the time required to reach that, a pH value of 7.2 was selected. After the samples were left standing at room temperature for 10 min, the phosphorescence was totally developed. The intensity was then measured at lambda(ex) = 282 nm and lambda(em) = 528 nm. The calibration graph was linear for 50-600 ng mL(-1) napropamide. The detection limit, according to the error propagation theory, was 16 ng mL(-1). The method has been demonstrated for the analysis of soils, peppers, and tomatoes, but, because of matrix interference, the method of standard additions was applied to determine napropamide in the vegetable samples. Recoveries from all these matrixes of added napropamide were near 100%.

Calibration↗

PubMed2006

Metal-enhanced phosphorescence: interpretation in terms of triplet-coupled radiating plasmons.

We report our detailed metal-enhanced phosphorescence (MEP) findings using Rose Bengal at low temperature. Silver Island Films (SiFs) in close proximity to Rose Bengal significantly enhance the phosphorescence emission intensity. In this regard, a 5-fold brighter phosphorescence intensity of Rose Bengal was observed from SiFs as compared to a glass control sample at 77 K. In addition, several factors affecting MEP, such as distance dependence and silver film morphology, were also investigated. Our findings suggest that both singlet and triplet states can couple to surface plasmons and enhance both fluorescence and phosphorescence yields. This finding suggests that MEP can be used to promote triplet-based assays, such as those used in photodynamic therapy.

Fluorescent Dyes↗

PubMed1999

Fluorescence and phosphorescence study of Tet repressor-operator interaction.

Fluorescence and phosphorescence measurements have been carried out on single-p tryptophan (Trp 43 or Trp 75)-containing mutants of Tet repressor (Tet R). Tet R containing Trp 43, the residue localized in the DNA recognition helix of the repressor, has been used to observe the binding of Tet R to two 20-bp DNA sequences of tet O1 and tet O2 operators. Binding of Tet R to tet O1 operator leads to a 78% decrease of the repressor fluorescence intensity, with an accompanying 20-nm blue shift of its fluorescence emission maximum to 330 nm. Upon binding of Tet R to tet O2 operator, the Trp 43 fluorescence intensity is quenched by 60%, and a 10-nm shift of its emission maximum to 340 nm occurs. Solute fluorescence quenching studies, using acrylamide, performed at low ionic strength indicate that in both the complex of Tet R with the O1 and that with the O2 operator, Trp 43 is moderately buried, as indicated by a bimolecular rate quenching constant of about 1.8 x 10(9) M(-1) sec(-1). In contrast to the Tet R-tet O2 complex, the Stern-Volmer acrylamide quenching constant Ksv of the complex with tet O1 operator changes from 7.5 M(-1) at 5 mM NaCl to 22 M(-1) at 200 mM NaCl, indicating different exposures of Trp 43 in the two complexes in solutions of higher ionic strength. Phosphorescence studies showed a 0-0 vibronic transition at 408 and 403 nm for Trp 43 and Trp 75, respectively. Upon binding of Tet R to the tet operators, we observed red shifts of 0-0 vibronic bands of Trp 43 to 413 and 412 nm for tet O1 and tet O2 operator, respectively, and the phosphorescence triplet lifetime of Trp 43 at 75 K was quenched from 6.0-5.5 to 3.5-3.3 sec. The thermal phosphorescence quenching profile ranged from -200 degrees C to -20 degrees C, and differed drastically for the two complexes, suggesting different dynamics of the microenvironment of the Trp 43 residue. The luminescence data for Trp 43 of Tet R suggest that the recognition helix of Tet R interacts in different fashions with the tet O1 and tet O2 operators.

Base Sequence↗

PubMed2001

Direct determination of naftopidil by non-protected fluid room temperature phosphorescence.

A selective and sensitive room temperature phosphorimetric method for the direct determination of naftopidil in biological fluids is described. The method is based on obtaining a phosphorescence signal from this antihypertensive drug using TlNO3 as a heavy atom perturber and Na2SO3 as a deoxygenator agent without a protective medium. This technique is named non-protected room temperature phosphorescence (NP-RTP), and enables us to determine analytes in complex matrices without the need for a tedious prior separation process. The optimization of Na2SO3 (8.5 x 10(-3) M) and the accurate value of pH (9.0) were determined using a simplex as a method of optimization. Sodium carbonate-hydrogencarbonate buffer solution (5.0 x 10(-2) M) was used to adjust the suitable pH. The optimum concentration of Tl+ (8.5 x 10(-2) M) was also determined. The delay time, gate time and time between flashes selected were 200 microseconds, 200 microseconds and 5 ms, respectively. Under the above conditions we propose a method to determine naftopidil by direct measurement of phosphorescence intensity with an emission wavelength of 526 nm and an excitation wavelength of 296 nm in the concentration range 0.05-1.00 mg L-1. Under these conditions the phosphorescence signal appears in 3 min once the sample has been prepared. Optimization of the various conditions permitted the establishment of an NP-RTP method for the determination with a detection limit, according to the error propagation theory, of 21.0 ng mL-1. The repeatability was studied using 10 solutions of 0.20 mg L-1 of naftopidil; if error propagation is assumed, the relative error is 1.39%. The standard deviation for replicate samples was 1.1 x 10(-2) mg L-1. This method was successfully applied to the determination of naftopidil, in human urine with recoveries between 106 and 112%.

Adrenergic alpha-Antagonists↗

PubMed2000

Phosphorescent porphyrin probes in biosensors and sensitive bioassays.

Platinum(II) and palladium(II) complexes of porphyrins and related tetrapyrrolic pigments emit strong phosphorescence at room temperatures, which is characterized by long lifetimes falling into the sub-millisecond range and long-wave spectral characteristics. These features make the dyes useful as probes for a number of bioanalytical applications, particularly those employing time-resolved fluorescent detection. They can provide high sensitivity and selectivity, together with rather simple instrumental set-up. A number of analytical systems are now under development that are based on the use of phosphorescent porphyrin probes. Experimental results are presented on the following systems: (i) fibre-optic phosphorescence lifetime-based oxygen sensor on the basis of hydrophobic platinum-porphyrins and development of advanced sensing materials and prototype instrumentation; (ii) practical applications of the optical oxygen sensor, including a sensitive immunosensor that employs glucose oxidase labels, a rapid screening method for cell viability in microtitre-plate format, non-destructive measurement of oxygen in packaged foods and reagentless biosensors for metabolites (glucose, lactate); and (iii) the use of water-soluble platinum- and palladium-porphyrins as labels for ultra-sensitive time-resolved phosphorescence immunoassays.

Biological Assay↗

PubMed2006

Theoretical study of phosphorescence in dye doped light emitting diodes.

Phosphorescence of platinum(II) octaethyl porphyrin (PtOEP), which has been used in organic light emitting diodes to overcome the efficiency limit imposed by the formation of triplet excitons, is studied by time-dependent (TD) density functional theory (DFT). The spin-orbit coupling (SOC) effects and the phosphorescence radiative lifetime (tau(p) (r)), calculated by the TD DFT method with the quadratic response technique, are analyzed for a series of porphyrins in order to elucidate the internal heavy atom effect on tau(p) (r). While the significance of the d(pi) orbital admixture into the lowest unoccupied molecular orbital e(g)(pi(*)), proposed by Gouterman et al. [J. Chem. Phys. 56, 4073 (1972)], is supported by our SOC calculations, we find that the charge-transfer (CT) mechanism is more important; the CT state of the (3)A(2g) symmetry provides effective SOC mixing with the ground state, and a large (3)A(2g)-(3)E(u) transition dipole moment gives the main contribution to the radiative phosphorescence rate constant. The IR and Raman spectra in the ground state and first excited triplet state (T(1)) are studied for proper assignment of vibronic patterns. An orbital angular momentum of the T(1) state is not quenched completely by the Jahn-Teller effect. A large zero-field splitting is predicted for PtP and PtOEP which results from a competition between the SOC and Jahn-Teller effects. A strong vibronic activity is found for the e(g) mode at 230 cm(-1) in PtP phosphorescence which is shifted to 260 cm(-1) in PtOEP. This out-of-plane vibration of the Pt atom produces considerable change of the SOC mixing. The role of charge-transfer state of d(pi)pi(*) type is stressed for the explanation of the electroluminescent properties of the dye doped light emitting diode.

Journal Article↗

PubMed1970

Influence of mercuric ions on the phosphorescence and photochemistry of DNA.

Partial mercuration of DNA, such that roughly one mercuric ion is bound for every two thymine residues, results in an enhancement of the phosphorescence by a factor of ten and a small enhancement of the photosteady thymine dimer yield. Complete mercuration of DNA [one Hg(II) added per momoner unit] results in quenching of the phosphorescence intensity and an inhibition of thymine dimer production. The enhancement of the phosphorescence is interpreted in terms of a heavy-atom effect caused by the preferential binding of Hg(II) to the thymine residues. The quenching of both the thymine phosphorescence and the rate of thymine dimerization upon complete mercuration is probably due to energy transfer from thymine to another base, presumably adenine, which when mercurated acts as an energy trap.

Binding Sites↗

PubMed1995

Solid matrix, room temperature phosphorescence identification and quantitation of the tetrahydrotetrols derived from the acid hydrolysis of benzo[a]pyrene-DNA adducts from human lung.

A new method, suitable for human biomonitoring, that uses room temperature phosphorescence for the detection of DNA damage by carcinogenic metabolites of polycyclic aromatic hydrocarbons is described. Samples of human lung DNA (1 mg) that had been subjected to immunoaffinity chromatography (anti-benzo[a]pyrene-diol-epoxide deoxyguanosine monoclonal antibodies) were acid hydrolyzed (0.1 N HCl, 90 degrees C, 3 h) and the resulting DNA lung hydrolyzates separated by high performance liquid chromatography. Relevant fractions were combined with a solid matrix support which consisted of a mixture of alpha-cyclodextrin (alpha-CD):NaCl (1:9) or alpha-CD:TINO3: aNO3 (1:1:8). The dried and powdered sample-matrix material was analyzed by phosphorescence spectroscopy at room temperature. Certain fractions of human lung samples were found to contain materials that yielded phosphorescence spectra that were indistinguishable from those produced when an authentic r-7, t-8, t-9, c-10-tetrahydroxy-7,8,9,10-tetrahydrobenzo[a]pyrene reference standard was analyzed. The data confirm previous studies that have reported the presence of r-7, t-8 dihydroxy-t-9,10-epoxy-7,8,9,10-tetrahydrobenzo[a]pyrene-DNA adducts in human tissues at levels of 1 adduct/10(7)-10(8) nucleotides. The alpha-cyclodextrin solid matrix, room temperature phosphorescence technique was performed with a commercially available instrument, but is 50 times more sensitive than the synchronous fluorescence spectroscopic technique previously used.

7,8-Dihydro-7,8-dihydroxybenzo(a)pyrene 9,10-oxide↗

PubMed1991

Tryptophan phosphorescence of G-actin and F-actin.

The tryptophan phosphorescence spectrum, intensity and decay kinetics of G-actin and F-actin were measured over a temperature range of 140-293 K. The fine structure in the phosphorescence spectra at low temperature, with O,O vibrational bands centered at 405 nm and 415.5 nm for both species, reveals a marked heterogeneity of the chromophore environment. The thermal quenching profile distinguishes these sites in terms of their flexibility, and shows that probably only one of the four tryptophan residues is still phosphorescent at ambient temperature due to its location in a relatively rigid buried core. Although some differences are demonstrated between G-actin and F-actin at low temperature, the identity of the triplet lifetime at ambient temperature strongly supports the notion that the conformation of the macromolecule is largely unaffected by polymerization. Preliminary phosphorescence anisotropy measurements demonstrate both the occurrence of singlet-singlet energy transfer among tryptophan residues and a strong immobilization of actin in the polymerized state.

Actins↗

PubMed1991

The mechanism of photosensitization in photodynamic therapy: phosphorescence behavior of porphyrin derivatives in saline solution containing human serum albumin.

The phosphorescence properties, especially the dynamic behavior of metal free and metal complexed porphyrins, have been studied in phosphate buffered saline (PBS) containing 0-3% human serum albumin (HSA). 6,7-Bisaspartyl-2,4-bis (1-hexyloxyethyl)-deutero- porphyrin (DP) and its gallium(III), zinc(II), and indium(III) complexes are used as photosensitizers. Upon irradiation, a solution of porphyrins containing more than 0.1% HSA shows phosphorescence with a lifetime longer than 1 ms. With an increase in irradiation time, phosphorescence intensities and lifetimes of porphyrins increase, depending upon their concentrations and triplet lifetimes, and approach saturated values close to those under deaerated conditions. The experimental results may be interpreted in terms of hypoxia induced by photosensitization in a local environment surrounding the sensitizer. The hypoxia is caused by the reaction between proteins and singlet molecular oxygen generated by photosensitization of porphyrins. Phosphorescence behavior of sensitizers in HSA PBS solution gives significant information for classifying photosensitizers as to their efficacy for photodynamic therapy.

Deuteroporphyrins↗

PubMed1988

Imaging of phosphorescence: a novel method for measuring oxygen distribution in perfused tissue.

The imaging of phosphorescence provides a method for monitoring oxygen distribution within the vascular system of intact tissues. Isolated rat lives were perfused through the portal vein with media containing palladium coproporphyrin, which phosphoresced and was used to image the liver at various perfusion rates. Because oxygen is a powerful quenching agent for phosphors, the transition from well-perfused liver to anoxia (no flow of oxygen) resulted in large increases of phosphorescence. During stepwise restoration of oxygen flow, the phosphorescence images showed marked heterogeneous patterns of tissue reoxygenation, which indicated that there were regional inequalities in oxygen delivery.

Animals↗

PubMed2001

Determination of macromolecular exchange and PO2 in the microcirculation: a simple system for in vivo fluorescence and phosphorescence videomicroscopy.

We have developed a system with two epi-illumination sources, a DC-regulated lamp for transillumination and mechanical switches for rapid shift of illumination and detection of defined areas (250-750 microm(2)) by fluorescence and phosphorescence videomicroscopy. The system permits investigation of standard microvascular parameters, vascular permeability as well as intra- and extravascular PO2 by phosphorescence quenching of Pd-meso-tetra (4-carboxyphenyl) porphine (PORPH). A Pechan prism was used to position a defined region over the photomultiplier and TV camera. In order to validate the system for in vivo use, in vitro tests were performed with probes at concentrations that can be found in microvascular studies. Extensive in vitro evaluations were performed by filling glass capillaries with solutions of various concentrations of FITC-dextran (diluted in blood and in saline) mixed with different amounts of PORPH. Fluorescence intensity and phosphorescence decay were determined for each mixture. FITC-dextran solutions without PORPH and PORPH solutions without FITC-dextran were used as references. Phosphorescence decay curves were relatively unaffected by the presence of FITC-dextran at all concentrations tested (0.1 microg/ml to 5 mg/ml). Likewise, fluorescence determinations were performed in the presence of PORPH (0.05 to 0.5 mg/ml). The system was successfully used to study macromolecular extravasation and PO2 in the rat mesentery circulation under controlled conditions and during ischemia-reperfusion.

Animals↗

PubMed1976

[Study of mouse liver cell phosphorescence at deep cooling].

The spectrum and decay curves of phosphorescence of mouse liver cells at --180 degrees C was studied using the phosphorescence microscope. The phosphorescence studied was shown to involve two components with different life spans. Part of either component in the total spectrum is estimated. A conclusion is made that at least two different centers (or groups of centers) exist in cells with the same spectral region of phosphorescence with highly diverging life times of triplet states.

Animals↗