一种液晶环氧树脂固化中扩散控制动力学研究

根据扩散控制反应的基本原理 ,建立了合适的反应模型 ,描述了 4 ,4′ 二 ( 2 ,3 环氧丙氧基 )偶氮苯(DGEAP) / 4,4′ 二氨基二苯甲烷 (DDM)环氧树脂的固化行为 .该模型认为 ,随着环氧基团反应程度的提高 ,基团的反应半径将受到影响 .当体系中出现了介晶基元的有序排列时 ,与之相连的反应基团的分布也受到影响 ,有序区内的局部浓度将变大 ,产生假浓度效应 ,并最终影响扩散控制反应动力学 .通过与普通环氧树脂固化动力学的比较 ,证实了这一效应 .     

A convenient and efficient preparation of β-substituted α-haloenones from diazodicarbonyl compounds

Rhodium(II)-catalyzed reactions of cyclic diazodicarbonyl compounds with a variety of halides have been examined. With acid halides, β-acyloxy α-haloenones are produced in good yields. With benzyl halides, β-benzyloxy α-haloenones are obtained in good yields. Reactions with methylene halides yield β-halomethoxy α-haloenones in good yields, whereas reactions with ethyl halides and ethylene dihalides result in β-hydroxy α-haloenones in high yields. These reactions provide a useful and rapid entry to β-substituted α-haloenones. The mechanistic pathway for the formation of these products has been also described in terms of halonium ylides.     

LC-ESI-MS Determination of Bilobalide and Ginkgolides in Canine Plasma

A sensitive and selective method using liquid chromatography with electrospray ionization mass spectrometric detection was developed for the quantification of bilobalide and ginkgolides in canine plasma. The analytes were extracted with diethyl ether-dichloromethane-isopropanol (6:3:1, v/v) after spiking the samples with daidzein (internal standard). The lower limit of quantification (LLOQ) of the method was 2.5 μg L⁻¹ for ginkgolide B and 10.0 μg L⁻¹ for bilabolide, ginkgolide A and ginkgolide C. The accuracy of the method was within 15% of the actual values over a wide range of plasma concentrations. The intra-day and inter-day precision was better than 15% (R.S.D.). Finally, the LC-ESI-MS method was successfully applied to study the pharmacokinetics of ginkgolides and bilabolide after administration of Ginkgo biloba extracts to dogs.     

2-甲基-6-对甲苯基-1,6-庚二烯的合成

以对甲苯乙酮(1)为原料,经烯醇硅醚化,Lewis酸催化Michael加成反应和Wittig反应,合成了新倍半萜烯化合物2-甲基-6-对甲苯基-1,6-庚二烯。     

An HPLC and EPR investigation on the stability of DMPO and DMPO spin adducts in vivo

Application of the spin trapping technique in intact animals requires an understanding of the stability and distribution of the spin traps and their spin adducts in vivo. We studied the stability of DMPO in vivo in mice using HPLC and the stability of spin adducts of DMPO by EPR in plasma, whole blood, peritoneal fluid, and homogenized heart tissue of the rat. At 15 minutes after intraperitoneal injection DMPO had similar concentrations in the liver, heart, and blood of the mice and 40% remained in the organs 2 hours after the injection. In contrast, the spin adduct DMPO-OH was short lived, with a half-life of 3.0 minutes in plasma, and was not detectable 1 minute after formation in whole blood and homogenized heart tissue. The carbon centered spin adduct DMPO-CH(OH)CH₃ was more stable, having half-lives of 16, 11, 3.6, and 0.79 minutes in plasma, peritoneal fluid, whole blood, and homogenized heart tissue, respectively. The spin adduct DMPO-SO₃ was sufficiently stable for the adduct to be observed directly from living mice.     

Characterization and epitope mapping of two monoclonal antibodies against human CD99

CD99 plays a critical role in the diapedesis of monocytes, T cell differentiation, and the transport of MHC molecules. Engagement of CD99 by agonistic monoclonal antibodies has been reported to trigger multifactorial events including T cell activation as well as cell-cell adhesion during hematopoietic cell differentiation. In this study, to identify the functional domains participating in the cellular events, we mapped the epitopes of CD99, which are recognized by two agonistic CD99 monoclonal antibodies, DN16 and YG32. Using recombinant fusion proteins of GST with whole or parts of CD99, we found that both antibodies interact with CD99 molecules independently of sugar moieties. DN16 mAb detected a linear epitope located in the amino terminal region of CD99 while YG32 mAb bound another linear epitope in the center of the extracellular domain. To confirm that the identified epitopes of CD99 are actually recognized by the two mAbs, we showed the presence of physical interaction between the mAbs and the fusion proteins or synthetic peptides containing the corresponding epitopes using surface plasmon resonance analyses. The dissociation constants of DN16 and YG32 mAbs for the antigen were calculated as 1.27 x 10(-7) and 7.08 x 10(-9) M, respectively. These studies will help understand the functional domains and the subsequent signaling mechanism of CD99.     

Intermolecular and intramolecular Diels-Alder cycloadditions of 3-ylidenepiperazine-2,5-diones and 5-acyloxy-2(1h)-pyrazinones

The 3-ylidenepiperazine-2,5-diones 16 and 39 and 5-acyloxy-2(1H)-pyrazinones 17 can serve as starting materials for the Diels-Alder reactions of alkenes and alkynes to the piperazine ring, under acidic conditions or in the presence of acetyl chloride, to afford tricyclic piperazine-2,5-diones 19, 20, 23-25, 27, 44, and 45. Intramolecular cycloadditions occur if 3-ylidenepiperazine-2,5-diones 30 and 32 are used as the starting materials. This procedure is a convenient path to bridged bicyclo[2.2.2]diazaoctane ring systems such as 31 and 33, the former being found in biologically active secondary mold metabolites, such as VM55599 (1) or brevianamide A (5), which have been isolated from various fungi. The synthesis of the indole compound 31 provided evidence for the proposed biochemical pathway with a Diels-Alder reaction as key step. Quantum chemical calculations have revealed that piperazinones with a cationic azadiene moiety are the most reactive species in Diels-Alder cycloadditions.     

Solid-phase synthesis of 4-biaryl-piperidine-4-carboxamides

A novel solid-phase synthesis of 4-biaryl-piperidine-4-carboxamides has been developed using FDMP resin with a carboxamide as the anchor point. With this approach, three points of diversity were incorporated into a GPCR-directed scaffold. Final products were obtained in good purity and yield.