Ni(2+)-modified gold nanoclusters for fluorescence turn-on detection of histidine in biological fluids

In this work, Ni(2+)-modified gold nanoclusters were fabricated for fluorescence turn-on detection of histidine. The fluorescence of Au NCs was first quenched by Ni(2+). Then, the addition of histidine can restore the fluorescence of Au NCs by binding with Ni(2+) and removing it from the surface of the Au NCs. This architecture ensured non-toxic, cost-effective, label-free and sensitive detection of histidine. The developed Au NCs-based fluorescent sensor offered high selectivity for histidine over other amino acids. The relative standard deviation (RSD) for eleven replicate detections was 2.7%. The detection limit for histidine is 30 nM. The recovery of spiked histidine in human urine samples ranges from 95 to 104%.     

Surface chemistry of ultrathin films of histidine on gold as probed by high-resolution synchrotron photoemission

Procedures for the vacuum deposition of thin histidine films on polycrystalline Au(111) and their characterization with high-resolution synchrotron-radiation-based photoelectron spectroscopy are reported. The chemical form of histidine (anionic vs zwitterionic) and the nature of its interactions with the substrate (strong ionic-covalent vs weak van der Waals bonding) in mono- and multilayer films are analyzed. It is shown that water adsorption on a pre-prepared histidine film at 100 K results in protonation of histidine molecules and partial formation of hydroxyl anions. These chemical effects are carefully differentiated from spectral changes associated with radiation damage of the histidine films.     

Monitoring the Hydrolysis of p—Nitrophenyl Acetate Catalyzed by Seryl—histidine with Electrospray Ionization Mass Spectrometry

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An indicator-displacement assay for naked-eye detection and quantification of histidine in human urine

A simple and efficient colorimetric method for the naked-eye detection and quantification of histidine in biological fluids was developed based on an indicator-displacement assay (IDA) and the Ni(2+)-histidine affinity pair. In this IDA approach, a commercially available dye, murexide, was used as the indicator and the selective detection of histidine was achieved based on the competition between indicator and histidine for the binding with Ni(2+). The competition of histidine with murexide for Ni(2+) resulted in an obvious color change of the solution from yellow to purple, and the permitted naked-eye detection of trace histidine. The developed bioassay allows the rapid, sensitive and selective detection of histidine in urine samples, and does not need complicated sample pretreatment. The detection limit was 0.4 μM with a linear range from 2 to 30 μM. The relative standard deviation for 11 replicate detections of 8 μM histidine was 2.0%. The developed sensor was successfully applied to the determination of histidine in human urine samples with recoveries from 97 to 105%.     

Carboxymethyl poly(L‐histidine) as a new pH‐sensitive polypeptide at endosomal/lysosomal pH

A carboxymethyl poly(L ‐histidine) has been synthesized as a new pH‐sensitive polypeptide at endosomal/lysosomal pH. Because of its poor water solubility at physiological pH, an application of poly(L ‐histidine) with a pK_a around 6.0 has been limited in spite of the native possession of the pH‐dependent property change at endosomal pH. Although the unmodified poly(L ‐histidine) suddenly precipitates out of the aqueous medium above pH 6.0 as the result of the deprotonation of the imidazole groups, the water solubility of the resulting carboxymethyl poly(L ‐histidine) has been improved at physiological pH. A solution turbidity measurement proved that no significant effect on a rapid aggregate formation or phase separation of serum proteins is induced by carboxymethyl poly(L ‐histidine). Hemolysis assay showed that the carboxymethyl poly(L ‐histidine) enhances membrane disruptive ability at endosomal/lysosomal pH. The cellular uptake of luciferase in the presence of the carboxymethyl poly(L ‐histidine) increases intracellular luciferase activity, which suggests that the carboxymethyl poly(L ‐histidine) makes the luciferase escape from lysosomal degradation. The carboxymethyl poly(L ‐histidine) would be the fundamental compound for designing various drug carriers with the pH sensitivity at endosomal/lysosomal pH. Copyright © 2007 John Wiley & Sons, Ltd.     

带电组氨酸侧链与DNA碱基间非键作用强度的理论研究

采用MP2方法和6-31+G(d,p)基组优化得到了带有一个正电荷的组氨酸侧链与4个DNA碱基间形成的18个氢键复合物的气相稳定结构, 从文献中获取了组氨酸侧链与DNA碱基间形成的12个堆积和T型复合物的气相稳定结构, 使用包含基组重叠误差(BSSE)校正的MP2方法和aug-cc-pVTZ基组及密度泛函理论M06-2X-D3方法和aug-cc-pVDZ基组计算了这些复合物的结合能. 研究结果表明, 包含BSSE校正的M06-2X-D3方法和aug-cc-pVDZ基组能够给出较准确的结合能; 气相条件下, 组氨酸侧链与同种DNA碱基间的离子氢键作用明显强于堆积作用和T型作用, 组氨酸侧链最易通过离子氢键与胞嘧啶C和鸟嘌呤G作用形成氢键复合物, 组氨酸与胞嘧啶C和鸟嘌呤G间的T型作用强于与腺嘌呤A和胸腺嘧啶T间的离子氢键作用; 水相条件下, 组氨酸侧链与同种DNA碱基间的离子氢键作用仍明显强于堆积作用和T型作用, 组氨酸侧链更易与胞嘧啶C和鸟嘌呤G相互作用形成氢键复合物, 但是最强的组氨酸侧链与胞嘧啶C间的T型作用明显弱于与腺嘌呤A和胸腺嘧啶T间的离子氢键作用, 说明水相条件下组氨酸侧链与DNA碱基间主要通过离子氢键作用形成氢键复合物.     

Studies on the Interactions between Potassium oxalato-oxodiperoxovanadate and Histidine by NMR and MS

K3[VO(O2)2(C2O4)]2H2O, (abbr. BpV (ox)) pertains to peroxovanadium (abbr. pV) complexes, which have been attracted considerable attention nowadays, since they are inhibitors of tyrosine phosphatase and may be developed into a new kind of drugs for the treatment of diabetes1. According to the evidence on water-biperoxovanadium, the molecular mechanism of insulin-like effects of pV involves in irreversibly oxidizing the catalytic cysteine at the active site of the target enzyme2,3. However…     

Selective fluorescence and naked eye detection of histidine in aqueous medium via hydrogen bonding assisted Schiff base condensation

Visible light excitable rhodamine B derivative (TARDHD) has been developed for fluorescence and naked eye detection of histidine in aqueous medium. TARDHD shows 45 fold fluorescence enhancement in the presence of histidine. It forms Schiff base with histidine and stabilizes via intra-molecular H-bonding. TARDHD can efficiently detect intracellular histidine.     

Reduction of Transient Histidine Radicals by Tyrosine: Influence of the Protonation State of Reactants

The role of tyrosine radicals as mediators of electron transfer reactions in enzymes is well established, as is the involvement of histidine as a binding partner. But how environmental factors affect these reactions remains poorly explored. In the study presented here, kinetic data on the influence of the protonation state of the reactants on the reduction of transient histidine radicals by tyrosine were obtained in neutral and basic aqueous solution (pH 6–12) using time-resolved chemically induced dynamic nuclear polarization (CIDNP). The histidine radicals were generated in the photo-induced reaction with the photosensitizer 3,3′,4,4′-tetracarboxy benzophenone. From model simulations of the detected CIDNP kinetics, pH dependent second-order rate constants of the reduction of histidine radicals were obtained for four possible combinations of the amino acids and their N-acetyl derivatives, and also for the systems histidine-phenylalanine dipeptide/N-acetyl tyrosine, and N-acetyl histidine/tyrosine-glutamine dipeptide. The pH dependences of the rate constant of the reduction reaction are explained accounting for the protonation states of reactants, and also protonation state of the equilibrium form of the product - reduced form of histidine radical, which is histidine with neutral or a positively charged imidazole.     

Selective labeling of histidine by a designed fluorescein-based probe

The synthesis of a novel fluorescent probe, 3-epoxypropoxy fluorescein (EPF), and its properties for labeling of histidine are described. The probe contained a fluorescein fluorophore with long-wavelength response and an active epoxy labeling group. In alkaline media EPF reacted selectively with histidine, rather than with other amino acids, causing a large increase in fluorescence intensity and thereby allowing a selective detection of histidine. This fluorescence increase resembled that of the fluorescein diaion with the increase of the media basicity, suggesting that the addition reaction of histidine with the epoxy group provides the fluorophore moiety with a basic molecular environment. As an application of this probe, fluorescent labeling of histidine in human serum was attempted and the obtained results were in agreement with those given by using histidine-nickel complex adsorptive voltammetry. Further, the relative S.D. of the method was 1.8% for 10 replicate determinations of 0.55 μM histidine. When 10 μM of EPF was used, the linear range for histidine was 0.007-10 μM with a detection limit (S/N=3) of 0.001 μM.     

Probing sites of histidine phosphorylation with iodination and tandem mass spectrometry

Phosphorylation at histidine residues occurs frequently in biology, but is often overlooked in proteomics experiments due to extreme acid lability. A new method utilizing histidine labeling with iodine to record information about phosphorylation is described. Essentially, phosphorylated histidine residues are not labeled while unmodified histidine undergoes complete iodination. Iodination is stabile both under acidic conditions, and upon collisional activation in the gas phase. This enables site-specific information to be retained with standard liquid chromatography separations and tandem mass spectrometry by collisional activation. Semi-quantitative information about the relative amounts of phosphorylated versus unmodified states can also be easily obtained from the relative ion abundances. This new method should provide a pathway forward for analyzing histidine phosphorylation in complex systems.     

Extraction and fluorometric microdetermination of histidine

A fluorometric method for the determination of the histidine in water samples is described. The histidine is first extracted with dichloromethane containing dibenzo-18-crown-6. The histidine is oxidized by bis(trifluoroacetoxy)iodobenzene to give a fluorescent product. The experimental variables and interferences in this determination are studied.     

Pre-resonance Raman and surface-enhanced Raman spectroscopy study of the complex of the antiviral and antiparkinsonian drug amantadine with histidine

UV-pre-resonance Raman spectroscopy (PRS) and surface-enhanced Raman spectroscopy (SERS) were applied to study the interaction of the antiviral and antiparkinsonian agent amantadine with histidine. The binding sites of amantadine and histidine molecules were identified in the complex. In this model, (i) the amino group of amantadine and the N1H group of histidine are included in the complex formation, (ii) the creation of the complex is mediated via formation of an H-bond between the nitrogen of the amantadine amino group and the hydrogen of the histidine N1H group. This model of the amantadine–histidine complex formation is discussed in the relation to a possible mode of interaction of the M2 protein transmembrane region with amantadine.     

Synthesis of para-sulfonatocalix[4]arene-modified silver nanoparticles as colorimetric histidine probes

This Communication reports a novel colorimetric sensor to probe histidine in water based on para-sulfonatocalix[4]arene-modified silver nanoparticles; this highly selective sensor allows a rapid quantitative assay of histidine down to a concentration of 5 x 10(-6) M, providing a new tool for the direct measurement of histidine.     

REVISED SPECTRA FOR THE INACTIVATION OF HAEMOPHILUS INFLUENZAE TRANSFORMING DNA BY MONOCHROMATIC ULTRAVIOLET LIGHT: EFFECT OF HISTIDINE

Abstract—It was reported previously that histidine sensitizes the genetic activity of Haemophilus influenzae transforming DNA to pure 334 nm ultraviolet light, Further measurements show that this apparent 334 nm sensitization was probably erroneous and that in fact, histidine protects DNA against inactivation by 334 nm light. This is now consistent with all previous observations that transforming DNA is protected by histidine against all near-UV wavelengths (above 320 nm) investigated.
A modified spectrum for the protection of H. influenza transforming DNA by histidine against ultraviolet light is described.     

Role of 2‐oxo and 2‐thioxo modifications on the proton affinity of histidine and fragmentation reactions of protonated histidine

A combination of electrospray ionisation (ESI), multistage and high‐resolution mass spectrometry experiments was used to compare the gas‐phase chemistry of the amino acids histidine (1), 2‐oxo‐histidine (2), and 2‐thioxo‐histidine (3). Collision‐induced dissociation (CID) of all three different proton‐bound heterodimers of these amino acids led to the relative gas‐phase proton affinity order of: histidine >2‐thioxo‐histidine >2‐oxo‐histidine. Density functional theory (DFT) calculations confirm this order, with the lower proton affinities of the oxidised histidine derivatives arising from their ability to adopt the more stable keto/thioketo tautomeric forms. All protonated amino acids predominately fragment via the combined loss of H₂O and CO to yield a₁ ions. Protonated 2 and 3 also undergo other small molecule losses including NH₃ and the imine HN=CHCO₂H. The observed differences in the fragmentation pathways are rationalised through DFT calculations, which reveal that while modification of histidine via the introduction of the oxygen atom in 2 or the sulfur atom in 3 does not affect the barriers against the loss of H₂O+CO, barriers against the losses of NH₃ and HN=CHCO₂H are lowered relative to protonated histidine. Copyright © 2010 John Wiley & Sons, Ltd.     

一种新的荧光素类荧光探针的设计合成及其对血清中组氨酸的选择性标记

组氨酸是人类必需的一种氨基酸 .它含有高反应活性的咪唑环 ,并在生物体系中金属离子的传输和神经递质的传送等方面起着重要的作用 [1,2 ] .所以 ,生物体液中组氨酸的选择性测定对生物化学的研究具有重要意义 .然而 ,由于各种氨基酸在结构及性质上的相似性 ,选择性测定单独的氨基酸常常需要借助如高效液相色谱和毛细管电泳等一些分离技术才能完成 .各种化合物的官能团反应可为一些高选择性的分子识别提供基础[3] .目前各种主体分子 ,包括荧光纳米探针和分子印迹聚合物等在生物分子的选择性识别方面发挥着重要的作用[4～ 6 ] .环氧氯丙烷作为…     

Flow Injection Analysis of Histidine with Enhanced Electrogenerated Chemiluminescence of Luminol

Histidine is one of the necessary basic amino acids in biological bases, which often controls the catalytic activity of enzymes and acts in holding the higher structure of proteins. Furthermore, it is also an important ingredient in pharmaceutical preparations used for treatment of hetpatosis and nephropathy. Therefore, the determination of histidine in biological fluids and pharmaceutical preparations is of great importance. Various methods have been proposed for the detection of histidine …     

Protonation processes and electronic spectra of histidine and related ions

A full structural assignment of the neutral, protonated, and deprotonated histidine conformers in the gas phase is presented. A total of 3024 unique trial structures were generated by all combinations of internal single-bond rotamers of these species and optimized at the B3LYP/6-311G* level and further optimized at the B3LYP/6-311++G** level. A set of unique conformers is found, and their relative energies, free energies, dipole moments, rotational constants, electron affinities, ionization energies, and harmonic frequencies are determined. The population ratio of histidine and its tautomer is 1:0.16 at 298 K. Massive conformational changes are observed due to protonation and deprotonation, and the intramolecular H-bonds are characterized with the atoms in molecules theory. The calculated proton dissociation energy, gas-phase acidity, proton affinity, and gas-phase basicity are in excellent agreement with the experiments. The deprotonation and protonation of gaseous histidine both occur on the imidazole ring, explaining the versatile biofunctions of histidine in large biomolecules. The UV spectra of neutral and singly and doubly protonated histidine are investigated with the TDDFT/B3LYP/6-311+G(2df,p) calculations. The S0-S1, S0-S2, and S0-S3 excitations of histidine are mixed pipi*/npi* transitions at 5.37, 5.44, and 5.69 eV, respectively. The three excitation energies for histidine tautomer are 4.85, 5.47, and 5.52 eV, respectively. The three excitations for protonated histidine are mainly npi* transitions at 5.45, 5.67, and 5.82 eV, respectively. The S0-S1 excitation of protonated histidine produces ImH-CbetaH2-CalphaH(COOH)-NH2+, while the S0-S2 and S0-S3 transitions produce ImH-CbetaH2-CalphaH(NH2)-(COOH)+. These data may help to understand the mechanisms of the UV fragmentation of biomolecules.