18 results on '"Mateo, C. R."'
Search Results
2. Development of a dual-analyte fluorescent sensor for the determination of bioactive nitrite and selenite in water samples
- Author
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Martínez-Tomé, M. J., Esquembre, R., Mallavia, R., and Mateo, C. R.
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- 2010
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3. Lateral heterogeneity in human platelet plasma membrane and lipids from the time-resolved fluorescence of trans-parinaric acid
- Author
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Mateo, C. R., Lillo, M. P., González-Rodríguez, J., and Acuña, A. U.
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- 1991
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4. Molecular order and fluidity of the plasma membrane of human platelets from time-resolved fluorescence depolarization
- Author
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Mateo, C. R., Lillo, M. P., González-Rodríguez, J., and Acuña, A. U.
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- 1991
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5. Selective recognition and imaging of bacterial model membranes over mammalian ones by using cationic conjugated polyelectrolytes.
- Author
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Kahveci, Z., Vázquez-Guilló, R., Mira, A., Martinez, L., Falcó, A., Mallavia, R., and Mateo, C. R.
- Subjects
POLYELECTROLYTES ,FLUORESCENCE ,FOOD industry ,LIPIDS ,CELL membranes ,BACTERIAL physiology - Abstract
The development of new tools for the detection and fluorescence imaging of bacteria is of great interest in clinical diagnosis and food and environmental safety. In this work, we have explored the ability of two cationic fluorene-based conjugated polyelectrolytes, HTMA-PFP and HTMA-PFNT, emitting in the blue and red spectral regions respectively, to selectively label bacterial over mammalian cells. With this end in view, vesicles with lipid compositions mimicking those of bacterial or mammalian membranes were used as model membranes to explore the interaction of the polyelectrolytes with both systems in samples containing either a single type of vesicle or a mixture of both. Changes in the intrinsic fluorescence of HTMA-PFP and HTMA-PFNT were used to quantify the affinity of these polyelectrolytes for the model lipid membranes, while quenching experiments were employed to evaluate their selectivity to each lipid system. In addition, fluorescence microscopy experiments were performed to check the ability of polyelectrolytes to label the vesicles without affecting their integrity. Results showed that both polyelectrolytes rapidly label the model vesicles but they preferentially bind to those mimicking bacterial membranes, HTMA-PFNT being much more selective to this type of membranes than HTMA-PFP. Preliminary experiments with living bacteria and mammalian cells support this conclusion, showing that in samples with both types of cells together, HTMA-PFNT only images the bacterial cells, thus evidencing its potential use for the selective recognition and imaging of bacterial presence. [ABSTRACT FROM AUTHOR]
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- 2016
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6. Toward new fluorescent bioinspired sensors: interaction of poly(fluorene-phenylene) with phospholipid bilayers.
- Author
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Mallavia, R., Paya, F. J., Salinas, A., Estepa, A., and Mateo, C. R.
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- 2007
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7. ChemInform Abstract: Rotational Dynamics of 1,6-Diphenyl-1,3,5-hexatriene and Derivatives from Fluorescence Depolarization.
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MATEO, C. R., LILLO, M. P., BROCHON, J. C., MARTINEZ-RIPOLL, M., SANZ-APARICIO, J., and ACUNA, A. U.
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- 1993
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8. Multienzymatic system immobilization in sol-gel slides: fluorescent superoxide biosensors development.
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Pastor I, Salinas-Castillo A, Esquembre R, Mallavia R, and Mateo CR
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- Antioxidants chemistry, Equipment Design, Equipment Failure Analysis, Phase Transition, Reproducibility of Results, Sensitivity and Specificity, Antioxidants analysis, Biosensing Techniques instrumentation, Enzymes, Immobilized chemistry, Multienzyme Complexes chemistry, Spectrometry, Fluorescence instrumentation, Superoxides chemistry
- Abstract
One of the potential areas of research in the development of biosensors is the production of analytical devices based on the use of immobilized multienzymatic systems. In this work, we report the development of three analytical systems for superoxide radical detection using sol-gel technology to immobilize enzyme systems. These systems are based on the connected reactions of three enzymes (xanthine oxidase, superoxide dismutase and horseradish peroxidase) coupled to the probe Amplex red. The difference between these three systems lies in the immobilization of two or three enzymes into a single or in different sol-gel slides. We check the potential use of each designed systems to quantify superoxide radical and potential evaluation of radical scavenging properties of several antioxidant compounds., (Copyright 2009 Elsevier B.V. All rights reserved.)
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- 2010
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9. Charge transport in luminescent polymers studied by in situ fluorescence spectroscopy.
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Montilla F, Pastor I, Mateo CR, Morallón E, and Mallavia R
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- Electrochemistry, Luminescence, Oxidation-Reduction, Polymers chemistry, Spectrometry, Fluorescence methods
- Abstract
Modulation of the photoluminescence of poly-[2,7-(fluorene)-1,4-(phenylene)] can be attained by reversible electrochemical modification of the conjugated chain (p- or n-doping). Controlled injection of charge quenches the fluorescent emission of the conjugated polymer. The injection of holes completely eliminates the emission, while the electrons only quench up to one-third of the initial fluorescence of the polymer. Analogous quenching effects have been previously reported for solid-state organoelectronic devices. Electrochemical Stern-Volmer plots permit the estimation of the relative mobility of charge carriers in the polymer layer. The mobility of holes is 1 order of magnitude higher that the mobility of electrons, as determined by this method.
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- 2006
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10. Membranotropic effects of the antibacterial agent Triclosan.
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Villalaín J, Mateo CR, Aranda FJ, Shapiro S, and Micol V
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- Calorimetry, Differential Scanning, Cell Membrane chemistry, Fluorescence Polarization, Humans, Membrane Lipids chemistry, Membranes, Artificial, Mouth microbiology, Porphyromonas gingivalis chemistry, Streptococcus sobrinus chemistry, X-Ray Diffraction, Anti-Infective Agents, Local pharmacology, Cell Membrane drug effects, Porphyromonas gingivalis drug effects, Streptococcus sobrinus drug effects, Triclosan pharmacology
- Abstract
Triclosan is a broad-spectrum hydrophobic antibacterial agent used in dermatological preparations and oral hygiene products. To gain further insight into the mode of action of Triclosan we examined its effects on membranes by performing leakage titrations of different oral bacteria and studying its interaction with model membranes through the use of different biophysical techniques. There was negligible efflux of intracellular material from Streptococcus sobrinus at the minimal inhibitory concentration of Triclosan; whatever leakage did occur commenced only at much higher concentrations. In contrast, no leakage was observed at even the minimal bactericidal concentration for Porphyromonas gingivalis. Triclosan decreased the onset temperature of the gel to liquid-crystalline phase transition of 1,2-dimyristoyl-sn-glycero-3-phosphocholine and 1,2-dimyristoyl-sn-3-[phospho-rac-glycerol] membranes and was immiscible with these lipids in the fluid phase at concentrations greater than 5 mol%. Steady-state fluorescence anisotropy measurements of different phospholipid/Triclosan samples using 3-(p-6-phenyl-1,3,5-hexatrienyl)-phenylpropionic acid were consistent with the calorimetric data. Incorporation of increasing amounts of Triclosan into 1,2-dielaidoyl-sn-glycero-3-phosphoethanolamine (DEPE) vesicles induced the nonlamellar H(II) hexagonal phase at low temperatures and new immiscible phases at temperatures below the main transition of DEPE. Taking these results together suggests that the antibacterial effects of Triclosan are mediated at least in part through its membranotropic effects, resulting in destabilized structures which compromise the functional integrity of cell membranes without inducing cell lysis., (Copyright 2001 Academic Press.)
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- 2001
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11. Effects of (+)-totarol, a diterpenoid antibacterial agent, on phospholipid model membranes.
- Author
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Micol V, Mateo CR, Shapiro S, Aranda FJ, and Villalaín J
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- Abietanes, Calorimetry, Differential Scanning, Cell Membrane chemistry, Cell Membrane drug effects, Dimyristoylphosphatidylcholine, Magnetic Resonance Spectroscopy, Phosphatidylglycerols, Temperature, X-Ray Diffraction, Anti-Infective Agents pharmacology, Diterpenes pharmacology, Lipid Bilayers chemistry
- Abstract
(+)-Totarol, a highly hydrophobic diterpenoid isolated from Podocarpus spp., is inhibitory towards the growth of diverse bacterial species. (+)-Totarol decreased the onset temperature of the gel to liquid-crystalline phase transition of DMPC and DMPG membranes and was immiscible with these lipids in the fluid phase at concentrations greater than 5 mol%. Different (+)-totarol/phospholipid mixtures having different stoichiometries appear to coexist with the pure phospholipid in the fluid phase. At concentrations greater than 15 mol% (+)-totarol completely suppressed the gel to liquid-crystalline phase transition in both DMPC and DMPG vesicles. Incorporation of increasing amounts of (+)-totarol into DEPE vesicles induced the appearance of the H(II) hexagonal phase at low temperatures in accordance with NMR data. At (+)-totarol concentrations between 5 and 35 mol% complex thermograms were observed, with new immiscible phases appearing at temperatures below the main transition of DEPE. Steady-state fluorescence anisotropy measurements showed that (+)-totarol decreased and increased the structural order of the phospholipid bilayer below and above the main gel to liquid-crystalline phase transition of DMPC respectively. The changes that (+)-totarol promotes in the physical properties of model membranes, compromising the functional integrity of the cell membrane, could explain its antibacterial effects.
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- 2001
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12. A fluorescence study of the interaction and location of (+)-totarol, a diterpenoid bioactive molecule, in model membranes.
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Mateo CR, Prieto M, Micol V, Shapiro S, and Villalaín J
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- Abietanes, Anisotropy, Dimyristoylphosphatidylcholine, Energy Transfer, Fatty Acids, Unsaturated chemistry, Fluorescent Dyes, Molecular Structure, Phospholipids chemistry, Spectrometry, Fluorescence, Temperature, Diterpenes chemistry, Lipid Bilayers chemistry, Membranes chemistry
- Abstract
(+)-Totarol, a diterpene extracted from Podocarpus totara, has been reported as a potent antioxidant and antibacterial agent. Although the molecular mechanism of action of this hydrophobic molecule remains unknown, recent work made in our laboratory strongly suggests that it could be lipid-mediated. Since (+)-totarol contains a phenolic ring, we have studied the intrinsic fluorescent properties of this molecule, i.e., quantum yield, lifetime, steady-state anisotropy and emission spectra, both in aqueous and in phospholipid phases, in order to obtain information on the interaction and location of (+)-totarol in biomembrane model systems. The phospholipid/water partition coefficient of (+)-totarol was found to be very high (K(p)=1.8x10(4)), suggesting that it incorporates very efficiently into membranes. In order to estimate the transverse location (degree of penetration) of the molecule in the fluid phase of DMPC model membranes, the spin labelled fatty acids 5-NS and 16-NS were used in differential quenching experiments. The results obtained show that (+)-totarol is located in the inner region of the membrane, far away from the phospholipid/water interface. Since (+)-totarol protects against oxidative stress, its interaction with an unsaturated fatty acid, trans-parinaric acid, was studied using fluorescence resonance energy transfer. No significant interactions were observed, molecules of trans-parinaric acid distributing themselves randomly amongst those of (+)-totarol in the phospholipid membrane.
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- 2000
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13. A coupled proton-transfer and twisting-motion fluorescence probe for lipid bilayers.
- Author
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Mateo CR and Douhal A
- Subjects
- Cholesterol, Fluorescent Dyes, Indicators and Reagents, Models, Chemical, Spectrometry, Fluorescence, Spectrophotometry, Atomic, Structure-Activity Relationship, Temperature, 1,2-Dipalmitoylphosphatidylcholine chemistry, Dimyristoylphosphatidylcholine chemistry, Lipid Bilayers chemistry
- Abstract
A new and sensitive molecular probe, 2-(2'-hydroxyphenyl)imidazo[1, 2-a]pyridine (HPIP), for monitoring structural changes in lipid bilayers is presented. Migration of HPIP from water into vesicles involves rupture of hydrogen (H) bonds with water and formation of an internal H bond once the probe is inside the vesicle. These structural changes of the dye allow the occurrence of a photoinduced intramolecular proton-transfer reaction and a subsequent twisting/rotational process upon electronic excitation of the probe. The resulting large Stokes-shifted fluorescence band depends on the twisting motion of the zwitterionic phototautomer and is characterized in vesicles of dimyristoyl-phosphatidylcholine and in dipalmitoyl-phosphatidylcholine at the temperature range of interest and in the presence of cholesterol. Because the fluorescence of aqueous HPIP does not interfere in the emission of the probe within the vesicles, HPIP proton-transfer/twisting motion fluorescence directly allows us to monitor and quantify structural changes within bilayers. The static and dynamic fluorescence parameters are sensitive enough to such changes to suggest this photostable dye as a potential molecular probe of the physical properties of lipid bilayers.
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- 1998
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14. Pressure effects on the lateral distribution of cholesterol in lipid bilayers: a time-resolved spectroscopy study.
- Author
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Tauc P, Mateo CR, and Brochon JC
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- Biophysical Phenomena, Biophysics, Fatty Acids, Unsaturated, Fluorescence Polarization, Fluorescent Dyes, Hydrostatic Pressure, Phosphatidylcholines chemistry, Temperature, Cholesterol chemistry, Lipid Bilayers chemistry
- Abstract
The effects of hydrostatic pressure and temperature on the phase behavior and physical properties of the binary mixture palmitoyloleoylphosphatidylcholine/cholesterol, over the 0-40 molar % range of cholesterol compositions, were determined from the changes in the fluorescence lifetime distribution and anisotropy decay parameters of the natural lipid trans-parinaric acid (t-PnA). Pressurized samples were excited with a Ti-sapphire subpicosecond laser, and fluorescence decays were analyzed by the quantified maximum entropy method. Above the transition temperature (T(T) = -5 degrees C), at atmospheric pressure, two liquid-crystalline phases, alpha and beta, are formed in this system. At each temperature and cholesterol concentration below the transition pressure, the fluorescence lifetime distribution pattern of t-PnA was clearly modulated by the pressure changes. Pressure increased the fraction of the liquid-ordered beta-phase and its order parameter, but it decreased the amount of cholesterol in this phase. Palmitoyloleoylphosphatidylcholine/cholesterol phase diagrams were also determined as a function of temperature and hydrostatic pressure.
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- 1998
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15. Distinct cholesterol and phospholipid incorporation at the platelet plasma membrane of hyperlipidemic subjects: structural order and function.
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García-Guerra R, Mateo CR, García-Muñoz MS, Zapata MA, Plaza I, and González-Rodríguez J
- Abstract
Plasma lipid composition, platelet aggregation, cholesterol (Ch)/glycoprotein IIb-IIIa (GP) and phospholipid (Ph)/GP molar ratios, fatty acid composition and structural order (1, 6-diphenyl-1, 3, 5-hexatriene (DPH) fluorescence anisotropy at 35 degrees C (r(DPH,35)) of human platelet plasma membranes (HPPM) were measured in four DPH,35 groups of hyperlipidemic patients (II: plasma Ch < 250 mg/dl and TG (triglycerides) <220 mg/dl, n = 21; III: Ch > 250 mg/dl and TG < 220 mg/dl, n = 23; IV: Ch < 250 mg/dl and TG > 220 mg/dl, n = 18; and V: Ch > 250 mg/dl and TG > 220 mg/dl, n = 12) and compared with those of the control group (I). Our results were: (i) in groups III, IV and V the HPPM (Ch + Ph)/GP molar ratio increased 7.0+/-7.7% (mean SD); (ii) the Ph/GP molar ratio increased significantly in groups III, IV and V, but most in IV and V, while the Ch/GP molar ratio increased only in groups III and V; (iii) the mean relative increase of Ch with respect to Ph in the HPPM of groups III, IV and V was 140% 21% and 54%, respectively; (iv) the Ch/GP molar ratio was correlated with LDL-Ch (0.41+/-0.16, P < 0.002, n = 55, for all the subjects and 0.60+/-0.11, P < 2.10(-4), n = 33, for subjects with TG < 220 mg/dl), however, it was totally uncorrelated with HDL-Ch; (v) the HPPM Ch/Ph molar ratio was positively correlated with plasma Ch (r = 0.51+/-0.08, P < 1.10(-6), n = 83) and with (LDL + HDL) Ch (r = 0.64+/-0.07, P < 1.10(-6), n = 73), the former correlation increased significantly ( r = 0.67+/-0.07, P < 1.10(-6), n = 53) when done only for subjects with TG < 220 mg/dl; (vi) the Ch/Ph molar ratio was only increased in group III (0.70+/-0.03, P < 3.10(-5), n = 23) and decreased in group IV (0.62+/-0.02, P < 0.001, n = 18); (vii) the fatty acid/GP molar ratio was significantly increased in groups IV and V, however, a significant absolute and relative increase of C16:0 and C18:1 was observed only in severe hypertriglyceridemia (> 500 mg/dl), together with a relative decrease of C18:0 and C20:4 ( n - 6); (viii) the HPPM structural order, as probed by r(DPH,35), was negatively correlated with DPH,35 plasma TG (r =- 0.61+/-0.10, P < 4.10(-5), n = 39), the Ph/GP molar ratio (r =-0.58+/-0.10, P < 2.10(-4), n = 39) and the the (C18:1 + C18:2))/GP molar ratio (r =- 0.80+/-0.05, P < 1.10(-6), n = 39), however, it was independent of plasma and HPPM Ch; (ix) the higher HPPM Ch/Ph molar ratio in group III was associated (r = 0.58+/-0.12, P < 0.005, n = 22) with a moderately higher platelet reactivity to collagen. We conclude that Ch and Ph were distinctly incorporated to HPPM in the different groups of hyperlipidemia and, therefore, that the absolute increase of Ch and Ph was more informative to understand the structural and functional modifications of the HPPM in hyperlipidemias, than the Ch/Ph molar ratio. On the other hand, the r was sensitive to the DPH,35 increase in the content of HPPM Ph and C18:1 + C18:2 and it was insensitive to the increase in the Ch content.
- Published
- 1998
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16. Structural features of phi29 single-stranded DNA-binding protein. I. Environment of tyrosines in terms of complex formation with DNA.
- Author
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Soengas MS, Mateo CR, Salas M, Acuña AU, and Gutierrez C
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- DNA Replication, Hydrogen-Ion Concentration, Solubility, Solvents, Spectrometry, Fluorescence, Temperature, Thermodynamics, Virus Replication, Bacillus Phages chemistry, DNA-Binding Proteins chemistry, Tyrosine chemistry, Viral Proteins chemistry
- Abstract
The single-stranded DNA-binding protein (SSB) of Bacillus subtilis phage phi29 is absolutely required for viral DNA replication in vivo. About approximately 95% of the intrinsic tyrosine fluorescence of phi29 SSB is quenched upon binding to ssDNA, making tyrosine residues strong candidates to be directly involved in complex formation with ssDNA. Thus, we have studied the spectroscopic properties of the phi29 SSB tyrosines (Tyr-50, Tyr-57, and Tyr-76) using steady-state and time-resolved fluorescence measurements. phi29 SSB tyrosines do not seem to be highly restricted by strong interactions with neighbor residues, as suggested by (i) the high value of the average quantum yield of the phi29 SSB fluorescence emission (phiF = 0.067 +/- 0.010), (ii) the fast motions of the tyrosine side chains (phi(short) = 0.14 +/- 0.06 ns), and (iii) the lack of tyrosinate emission at neutral pH. Stern-Volmer analysis of the quenching by acrylamide and I- indicates that phi29 SSB tyrosines are surrounded by a negatively charged environment and located in a relatively exposed protein domain, accessible to the solvent and, likely, to ssDNA. Changes in the intrinsic fluorescence upon ssDNA binding allowed us to determine that temperature has an opposite effect on the thermodynamic parameters K (intrinsic binding constant) and omega (cooperativity) defining phi29 SSB-poly(dT) interaction, the effective DNA binding constant, K(eff) = K omega, being largely independent of temperature. Altogether, the fluorescent properties of phi29 SSB tyrosines are consistent with a direct participation in complex formation with ssDNA.
- Published
- 1997
- Full Text
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17. Structural features of phi29 single-stranded DNA-binding protein. II. Global conformation of phi29 single-stranded DNA-binding protein and the effects of complex formation on the protein and the single-stranded DNA.
- Author
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Soengas MS, Mateo CR, Rivas G, Salas M, Acuña AU, and Gutiérrez C
- Subjects
- Chemical Phenomena, Chemistry, Physical, Circular Dichroism, Hydrogen-Ion Concentration, Macromolecular Substances, Protein Conformation, Temperature, Viral Proteins chemistry, Bacillus Phages chemistry, DNA, Single-Stranded chemistry, DNA-Binding Proteins chemistry
- Abstract
The strand-displacement mechanism of Bacillus subtilis phage phi29 DNA replication occurs through replicative intermediates with high amounts of single-stranded DNA (ssDNA). These ssDNA must be covered by the viral ssDNA-binding protein, phi29 SSB, to be replicated in vivo. To understand the characteristics of phi29 SSB-ssDNA complex that could explain the requirement of phi29 SSB, we have (i) determined the hydrodynamic behavior of phi29 SSB in solution and (ii) monitored the effect of complex formation on phi29 SSB and ssDNA secondary structure. Based on its translational frictional coefficient (3.5 +/- 0.1) x 10(8) gs(-1), and its rotational correlation time, 7.0 +/- 0.5 ns, phi29 SSB was modeled as a nearly spherical ellipsoid of revolution. The axial ratio (p = a/b) could range from 0.8 to 1.0 (oblate model, a < b) or 1.0 to 3.2 (prolate model, a > b). Far-UV CD spectra, indicated that phi29 SSB is highly organized within a wide range of temperatures (15 to 50 degrees C), being mainly constituted by beta-sheet elements (approximately 50%, at pH 7). Complex formation with ssDNA, although inducing minimal changes on the global conformation of phi29 SSB, had a clear stabilizing effect against pH and temperature increase of the solution samples. On the other hand, phi29 SSB binding leads to non-conservative changes of the near-UV CD spectra of ssDNA, which are consistent with different nearest-neighbor interactions of the nucleotide bases upon complex formation. The above results will be compared to those reported for other SSBs and discussed in terms of the functional roles of phi29 SSB.
- Published
- 1997
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18. New fluorescent octadecapentaenoic acids as probes of lipid membranes and protein-lipid interactions.
- Author
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Mateo CR, Souto AA, Amat-Guerri F, and Acuña AU
- Subjects
- 1,2-Dipalmitoylphosphatidylcholine chemistry, Calorimetry, Cell Membrane ultrastructure, Dimyristoylphosphatidylcholine chemistry, Energy Transfer, Fluorescence Polarization methods, Gels, Humans, Isomerism, Kinetics, Molecular Conformation, Protein Binding, Spectrometry, Fluorescence methods, Tryptophan, Ultrasonography, Blood Platelets diagnostic imaging, Fatty Acids, Unsaturated, Fluorescent Dyes, Gramicidin chemistry, Lipid Bilayers chemistry, Liposomes chemistry, Phosphatidylcholines chemistry, Protein Structure, Secondary, Proteins chemistry
- Abstract
The chemical and spectroscopic properties of the new fluorescent acids all(E)-8, 10, 12, 14, 16-octadecapentaenoic acid (t-COPA) and its (8Z)-isomer (c-COPA) have been characterized in solvents of different polarity, synthetic lipid bilayers, and lipid/protein systems. These compounds are reasonably photostable in solution, present an intense UV absorption band (epsilon(350 nm) approximately 10(5) M(-1) cm(-1)) strongly overlapped by tryptophan fluorescence and their emission, centered at 470 nm, is strongly polarized (r(O) = 0.385 +/- 0.005) and decays with a major component (85%) of lifetime 23 ns and a faster minor one of lifetime 2 ns (D,L-alpha-dimyristoylphosphatidylcholine (DMPC), 15 degrees C). Both COPA isomers incorporate readily into vesicles and membranes (K(p) approximately 10(6)) and align parallel to the lipids. t-COPA distributes homogeneously between gel and fluid lipid domains and the changes in polarization accurately reflect the lipid T(m) values. From the decay of the fluorescence anisotropy in spherical bilayers of DMPC and POPC it is shown that t-COPA also correctly reflects the lipid order parameters, determined by 2H NMR techniques. Resonance energy transfer from tryptophan to the bound pentaenoic acid in serum albumin in solution, and from the tryptophan residues of gramicidin in lipid bilayers also containing the pentaenoic acid, show that this probe is a useful acceptor of protein tryptophan excitation, with R(O) values of 30-34 A.
- Published
- 1996
- Full Text
- View/download PDF
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