Cr,Fe,Cu/Al2O3界面化学结构的光电子能谱

应用Ｘ－射线光电子能谱，通过离子刻蚀，原位研究第四周期过渡金属与氧化铝所形成界面的化学状态，结果表明，Ｃｒ，Ｆｅ在界面处有不同程度的氧化，氧化程度Ｃｒ＞Ｆｅ，而Ｃｕ则无明显氧化。化学成份的定量分析表明，界面过渡层的厚度与界面化学反应强弱直接相关。     

Molecular simulation of surfactant-assisted protein refolding

Protein refolding to its native state in vitro is a challenging problem in biotechnology, i.e., in the biomedical, pharmaceutical, and food industry. Protein aggregation and misfolding usually inhibit the recovery of proteins with their native states. These problems can be partially solved by adding a surfactant into a suitable solution environment. However, the process of this surfactant-assisted protein refolding is not well understood. In this paper, we wish to report on the first-ever simulations of surfactant-assisted protein refolding. For these studies, we defined a simple model for the protein and the surfactant and investigated how a surfactant affected the folding behavior of a two-dimensional lattice protein molecule. The model protein and model surfactant were chosen such that we could capture the important features of the folding process and the interaction between the protein and the surfactant, namely, the hydrophobic interaction. It was shown that, in the absence of surfactants, a protein in an "energy trap" conformation, i.e., a local energy minima, could not fold into the native form, which was characterized by a global energy minimum. The addition of surfactants created folding pathways via the formation of protein-surfactant complexes and thus enabled the conformations that fell into energy trap states to escape from these traps and to form the native proteins. The simulation results also showed that it was necessary to match the hydrophobicity of surfactant to the concentration of denaturant, which was added to control the folding or unfolding of a protein. The surfactants with different hydrophobicity had their own concentration range on assisting protein refolding. All of these simulations agreed well with experimental results reported elsewhere, indicating both the validity of the simulations presented here and the potential application of the simulations for the design of a surfactant on assisting protein refolding.     

Four New Lariciresinol‐Based Lignan Glycosides from the Roots of Rhus javanica var. roxburghiana

The four new lariciresinol‐based lignan glycosides, (?)‐lariciresinol 4′‐(6″‐O‐feruloyl‐β‐D ‐glucopyranoside) ( 1 ), (?)‐lariciresinol 4′‐(4″,6″‐di‐O‐feruloyl‐β‐D ‐glucopyranoside) ( 2 ), 5,5′‐dimethoxylariciresinol 4′‐(4″,6″‐di‐O‐feruloyl)‐β‐D ‐glucopyranoside) ( 3 ), and 4‐O‐[α‐(1,2‐dihydroxyethyl)syringyl]‐5,5′‐dimethoxylariciresinol 4′‐(4″,6″‐di‐O‐feruloyl‐β‐D ‐glucopyranoside) ( 4 ), together with two known ones, lariciresinol 4′‐β‐D ‐glucopyranoside) ( 5 ) and tortoside B ( 6 ), were isolated from the BuOH extract of Rhus javanica var. roxburghiana roots, and their structures were established by means of various spectroscopic techniques.     

Fast protein analysis enabled by high-temperature hydrolysis

While the bottom-up protein analysis serves as a mainstream method for biological studies, its efficiency is limited by the time-consuming process for enzymatic digestion or hydrolysis as well as the post-digestion treatment prior to mass spectrometry analysis. In this work, we developed an enzyme-free microreaction system for fast and selective hydrolysis of proteins, and a direct analysis of the protein digests was achieved by nanoESI (electrospray ionization) mass spectrometry. Using the microreactor, proteins in aqueous solution could be selectively hydrolyzed at the aspartyl sites within 2 min at high temperatures (∼150 °C). Being free of salts, the protein digest solution could be directly analyzed using a mass spectrometer with nanoESI without further purification or post-digestion treatment. This method has been validated for the analysis of a variety of proteins with molecular weights ranging from 8.5 to 67 kDa. With introduction of a reducing agent into the protein solutions, fast cleavage of disulfide bonds was also achieved along with high-temperature hydrolysis, allowing for fast analysis of large proteins such as bovine serum albumin. The high-temperature microreaction system was also used with a miniature mass spectrometer for the determination of highly specific peptides from Mycobacterium tuberculosis antigens, showing its potential for point-of-care analysis of protein biomarkers.

A high-temperature microreaction system is developed for fast and selective hydrolysis of proteins, enabling direct analysis of protein biomarkers by mass spectrometry.     

近5年化学奥林匹克(初赛)试题的分析及建议

从化学核心素养出发，分析近5年化学奥林匹克（初赛）试题考查的学生知识水平、能力水平、素养水平，并针对培养中学生核心素养的教学实践提出建议。     

Two Novel Oxamidato-bridged Tetranuclear Complexes M[Cu(PMoxd)]3(ClO4)2 (M=Mn, Ni, Cu(PMoxd)=N,N′-bis(pyridyl-methyl)-oxamidatocopper(II)): Syntheses, Spectra, Magnetic and Electrochemical Properties

Two novel oxamidato-bridged Mn[Cu(PMoxd)]₃(ClO₄)₂ (1) Ni[Cu(PMoxd)]₃(ClO₄)₂ (2) tetranuclear complexes were prepared and characterized by i.r., e.p.r., electronic spectra, cyclic voltammograms, and magnetic properties. The magnetic analysis was carried out by means of the theoretical expression of the magnetic susceptibility deduced from the spin Hamiltonian H=−2JS_M(S_Cu1+ S_Cu2 + S_Cu3) (M=Mn, Ni), leading to J=−20.4 cm⁻¹; −121.1 cm⁻¹ for complexes (1) and (2) respectively. Magnetic measurements indicate that the overall magnetic behavior of the tetranuclear species are antiferromagnetic.     

利血平的光化学荧光特性及其应用

在10％HAc介质中,利血平经紫外光照射时,其光化学反应产物具有强烈荧光(λ_(ax)=385 nm,λ_(ax)=490 nm)。利血平浓度在0.01～0.30μg/ml范围内,荧光强度与浓度呈良好的线性关系,由此建立了利血平的光化学荧光测定法。方法的检出限为1.3 ng/ml,相对标准偏差为1.6％。本法简便快速且灵敏度高,可用于片剂及注射液中利血平含量的测定。     

Study of organohalogen contaminants in yogurt by NAA and GC-ECD

The concentrations and distributions of total halogen (TX), extractable organohalogen (EOX) and extractable persistent organohalogen (EPOX) were determined in 20 kinds of yogurt specimens collected from Chinese supermarkets using neutron activation analysis (NAA) and gas chromatography equipped with a ⁶³Ni electron capture detector (GC-ECD). The results indicated that the halogens in yogurt mainly existed as non-extractable organohalogen compounds. About 25–30% of EOX was EPOX. EOCl and EPOCl were the main organohalogen species in yogurt. The average concentration of the identified organochlorine, such as organochlorine pesticides (OCPs) and polychlorinated biphenyls (PCBs), was below 4% of EPOCl.     

Improvement of cyclosporin A determination in whole blood by reversed-phase high-performance liquid chromatography

A chromatographic method was developed for the determination of cyclosporin A in human whole blood using reversed-phase HPLC at room temperature. Most previous reports carried out this liquid chromatographic separation at temperatures above 70 degrees C. The present procedure greatly improves the detection limit by controlling peak broadening effects, as well as the lifetime of the column at room temperature. Under optimal conditions and using ketoconazole as an internal standard, the calibration graph was linear in the range of 16-1000 microg/L with a relative standard deviation of 3.72% at 150 microg/L and 2.45% at 300 microg/L (n = 11) of cyclosporin A. The detection limit was of 5.0 microg/L cyclosporin A. By this procedure, cyclosporin A pharmacokinetic parameters in healthy Chinese subjects were studied. The developed method could be applied to the quantification of cyclosporin A in human blood samples and allows the study of its pharmacokinetics in routine laboratories.     

Accurate redetermination of the X-ray structure and electronic bonding in adenosylcobalamin

The electronic structure of adenosylcobalamin (B12 coenzyme, AdoCbl) has been calculated by a density functional method, using the orthogonalized linear combination of the atomic orbital method (OLCAO). Since a fixed accurately determined geometry was needed in such calculations, the crystal structure of adenosylcobalamin has been redone and refined to R = 0.065, using synchrotron diffraction data. Comparison with the recently reported electronic structures of cyano- (CNCbl) and methylcobalamin (MeCbl) shows that the net charges and bond orders vary only on the axial donors. The values in the three cobalamins suggest that the Co-C bond in MeCbl has a strength similar to that in AdoCbl, but it is significantly weaker that that in CNCbl. Present results are compared with those previously reported for the analogous corrin derivatives; i.e., simplified cobalamins with the side chains a-f replaced by H atoms. Despite a qualitative agreement, a discrepancy in the calculated HOMO-LUMO gap is found.