Your browser doesn't support javascript.
loading
Show: 20 | 50 | 100
Results 1 - 5 de 5
Filter
Add more filters










Database
Language
Publication year range
1.
Talanta ; 74(4): 526-32, 2008 Jan 15.
Article in English | MEDLINE | ID: mdl-18371671

ABSTRACT

A novel method is proposed in this paper, that is the silver nanoparticle (nanoAg)-cetyltrimethylammonium bromide (CTMAB) is used as the probe of resonance light scattering (RLS) for the determination of nucleic acids. Under optimum conditions, there are linear relationships between the quenching extent of RLS and the concentration of nucleic acids in the range of 4.0x10(-9)-2.0x10(-6)gmL(-1) for fish sperm DNA (fsDNA), 7.0x10(-9)-1.8x10(-6)gmL(-1) for calf thymus DNA (ctDNA) and 6.0x10(-9)-1.0x10(-6)gmL(-1) for yeast RNA (yRNA). The detection limits (S/N=3) of fsDNA, ctDNA and yRNA are 2.7x10(-10)gmL(-1), 4.8x10(-10)gmL(-1) and 7.2x10(-10)gmL(-1), respectively. The studies indicate that there are interactions among nanoAg, CTMAB and fsDNA through electrostatic and chemical affinity, and the nanoAg-CTMAB complex can induce the structural change of base stacking and helicity of fsDNA.


Subject(s)
Cetrimonium Compounds/chemistry , Metal Nanoparticles , Nucleic Acids/chemistry , Silver/chemistry , Calibration , Cetrimonium , Hydrogen-Ion Concentration , Sensitivity and Specificity
2.
J Fluoresc ; 17(6): 721-6, 2007 Nov.
Article in English | MEDLINE | ID: mdl-17703351

ABSTRACT

In this paper, the interaction between florasulam (FU, 2',6',8-trifluoro-5-methoxy [Kragh-Hansen U, Molecular aspects of ligand binding to serum albumin. Pharmacol Rev 33(1):17-53 1981; Carter DC and Ho JX, Structure of serum albumin. Adv Protein Chem 45:153-203 1994; He XM, and Carter DC, Atomic structure and chemistry of human serum albumin. Nature 358(6383):209-215 1992] triazolo [1,5-c]pyrimidine-2-sulfonanilide) and bovine serum albumin (BSA) was investigated by fluorescence, ultraviolet absorption (UV) and Far-UV circular dichroism (CD) spectrometries. A strong fluorescence quenching was observed and the quenching mechanism was considered as static quenching. The binding constant of FU with BSA at 299 and 309 K were obtained as 1.5 x 10(4) and 7.1 x 10(3) l mol(-1), respectively. There was one binding site between FU and BSA. The thermodynamic parameters enthalpy change (DeltaH) and entropy change (DeltaS) were calculated as -57.89 kJ mol(-1) and -113.6 J mol(-1) K(-1), respectively, which indicated that the acting force between FU and BSA was mainly hydrogen bond and Van der Waals force. According to the Förster non-radiation energy transfer theory, the average binding distance between donor (BSA) and acceptor (FU) was obtained (r = 1.59 nm). The investigations of the UV/Vis and CD spectra of the system showed that the conformation of BSA was changed in presence of FU.


Subject(s)
Pyrimidines/chemistry , Serum Albumin, Bovine/chemistry , Sulfonamides/chemistry , Animals , Binding Sites , Cattle , Circular Dichroism , Energy Transfer , In Vitro Techniques , Protein Conformation , Pyrimidines/metabolism , Serum Albumin, Bovine/metabolism , Spectrometry, Fluorescence , Spectrophotometry, Ultraviolet , Sulfonamides/metabolism , Thermodynamics , Tryptophan/chemistry
3.
Anal Chim Acta ; 596(1): 16-22, 2007 Jul 16.
Article in English | MEDLINE | ID: mdl-17616235

ABSTRACT

It was found that oxolinic acid (OA) at high concentration can self-assemble into nano- to micro-meter scale OA aggregates in Tris-HCl (pH 7.48) buffer solution. The nanoparticles of OA were adopted as fluorescence probes in the quantitative analysis of proteins. Under optimum conditions, the fluorescence quenching extent of nanometer scale OA aggregates was in proportion to the concentration of albumins in the range of 3.0x10(-8) to 3.0x10(-5) g mL(-1) for bovine serum albumin (BSA) and 8.0x10(-8) to 8.0x10(-6) g mL(-1) for human serum albumin (HSA). The detection limits (S/N=3) were 3.4x10(-9) g mL(-1) for BSA, and 2.6x10(-8) g mL(-1) for HSA, respectively. Samples were satisfactorily determined. The interaction mechanism of the system was studied using fluorescence, UV-vis, resonance light scattering (RLS) and transmission electron microscope (TEM) technology, etc., indicating that the nonluminescent complex was formed between serum albumin molecular and OA, to disaggregate the self-association of OA, which resulted in the dominated static fluorescence quenching in the system.


Subject(s)
Fluorescent Dyes/chemistry , Oxolinic Acid/chemistry , Serum Albumin, Bovine/analysis , Serum Albumin, Bovine/chemistry , Spectrometry, Fluorescence/methods , Amino Acids/chemistry , Animals , Buffers , Cattle , Fluorescence , Humans , Hydrogen-Ion Concentration , Light , Luminescent Measurements , Metals/chemistry , Microscopy, Electron, Transmission , Nanoparticles/chemistry , Scattering, Radiation , Serum Albumin/analysis , Serum Albumin/chemistry
4.
Spectrochim Acta A Mol Biomol Spectrosc ; 65(3-4): 543-8, 2006 Nov.
Article in English | MEDLINE | ID: mdl-16644263

ABSTRACT

It is found that nucleic acids can enhance the fluorescence intensity of yttrium(III) (Y(3+))-rutin in presence of cetyltrimethylammonium bromide (CTMAB) system. In hexamethylenetetramine (HMTA)-HCl buffer, the maximum enhanced fluorescence is produced, with maximum excitation and emission wavelengths at 452 and 520 nm, respectively. Based on this, a new fluorimetric method of determination of nucleic acids is proposed. Under optimum conditions, the enhanced fluorescence intensity is proportion to the concentration of nucleic acids in the range of 1.0 x 10(-7) to 1.0 x 10(-5)g/ml for fish sperm DNA (fsDNA), 1.0 x 10(-7) to 4.6 x 10(-6)g/ml for yeast RNA (yRNA), their detection limits (S/N=3) are 7.5 x 10(-8), 8.0 x 10(-8)g/ml, respectively. The interaction mechanism is also studied.


Subject(s)
Cetrimonium Compounds/chemistry , DNA/analysis , RNA/analysis , Rutin/chemistry , Spectrometry, Fluorescence/methods , Yttrium/chemistry , Animals , Cetrimonium , Fishes/genetics , Fluorescence , Male , RNA, Fungal/analysis , Spermatozoa/chemistry , Yeasts/genetics
5.
Luminescence ; 21(3): 129-34, 2006.
Article in English | MEDLINE | ID: mdl-16502393

ABSTRACT

Nucleic acids can quench resonance light scattering (RLS) intensity of the Y(III)-1,6-bi(1'-phenyl-3'-methyl-5'-pyrazolone-4'-)hexane-dione(BPMPHD) complex in the pH range 5.0-5.8. Under optimal conditions, there are linear relationships between the quenching of RLS and the concentration of nucleic acids in the range 6.3 x 10(-8)-2.1 x 10(-5) g/mL for fish sperm DNA (fsDNA), 1.2 x 10(-8)-5.0 x 10(-5) g/mL for calf thymus DNA (ctDNA) and 6.0 x 10(-8)-2.0 x 10(-5) g/mL for yeast RNA (yRNA). The detection limits (3 s) of fsDNA, ctDNA and yRNA are 0.7 ng/mL, 3.8 ng/mL and 4.2 ng/mL, respectively.


Subject(s)
Aldehydes/chemistry , Nucleic Acids/analysis , Nucleic Acids/chemistry , Pyrazoles/chemistry , Scattering, Radiation , Animals , Cattle , DNA/analysis , DNA/chemistry , Fishes , Hydrogen-Ion Concentration , Male , RNA/analysis , RNA/chemistry , Sensitivity and Specificity , Spermatozoa/metabolism , Thymus Gland/metabolism , Yeasts/metabolism
SELECTION OF CITATIONS
SEARCH DETAIL
...