物理改性对PP成型收缩性的影响

研究了物理改性对聚丙烯(PP)成型收缩率的影响效果及其作用机理。研究表明,填充、共混、增强改性均可降低PP的成型收缩率。填充改性通过改变PP的结构状态影响PP的成型收缩率,且片状的滑石粉有较好的效果;共混改性通过使共混组分的分子链相互缠绕,改变PP的结晶从而控制PP的成型收缩率,与高密度聚乙烯相比,线性低密度聚乙烯对PP成型收缩率的影响较显著;玻璃纤维(GF)增强改性PP除了起到破坏PP的结晶度,从而影响成型收缩率外,更重要的是GF的加入限制了PP的结晶收缩。     

马来酸酐接枝EPDM改性聚丙烯的制备及性能研究

采用聚丙烯(PP)为母体材料,三元乙丙橡胶(EPDM)和三元乙丙橡胶接枝马来酸酐(EDPM-g-MAH)作为增韧剂改性PP,制备共混材料。研究结果表明:与纯EPDM改性PP相比较,EPDM-g-MAH改性PP获得的共混材料的性能更佳,具有良好的弯曲模量及冲击强度,维卡软化点显著降低,对于材料的耐热性的提高具有一定作用。同时在PP/EPDM-g-MAH共混材料的冲击断裂表面发现较为粗糙的结构,表明EPDM-g-MAH作为增韧剂填充PP,对于提高PP的韧性,提高材料的抗冲击性能具有明显的作用。     

动态硫化聚丙烯／三元乙丙橡胶共混材料

采用动态硫化技术研制了聚丙烯/三元乙丙橡胶共混材料(PP/EPDM)。考察了EPDM含量对共混材料力学性能、热性能的影响,研究了共混材料的流变性能,以及注射成型工艺条件与成型收缩率之间的关系。     

聚丙烯微孔发泡材料制备及改性进展

聚丙烯(PP)微孔发泡材料具有质轻、力学性能较高的特点,PP基体性质、发泡剂种类、发泡制备成型工艺、化学改性方法、共混及填充改性等方法均可以影响发泡材料的泡孔结构及发泡材料的性能。综述了PP微孔发泡材料的制备成型工艺、化学、共混、纳米、填充等改性方法研究进展,指出采用成本低廉、无毒的化学类发泡剂制备泡孔结构良好的PP微孔发泡材料将是今后研究的热点。PP的交联及接枝改性技术,与其它聚合物、填料共混技术是改善泡孔结构、提高泡沫材料发泡性能和力学性能的途径,研究改性材料与PP基体材料的界面相容性问题也是今后的研究方向。     

PP三元填充共混体系力学性能的研究

研究了乙烯-醋酸乙烯共聚物(EVA)、HDPE、LLDPE、PS、氯化聚乙烯(CPE)和丙烯酸酯类共聚物(ACR)等6种聚合物分别组成的PP/滑石粉/聚合物三元填充共混体系的缺口冲击强度、拉伸强度、断裂伸长率、拉伸弹性模量、球压痕硬度、成型收缩率及熔体流动速率等性能。结果表明:EVA、CPE和PS对PP/滑石粉二元填充体系的改性效果明显。     

超高分子量聚乙烯/聚丙烯共混改性研究进展

超高分子量聚乙烯(UHMWPE)的加工一直是一个世界性难题。采用聚丙烯(PP)改性UHMWPE可显著提高UHMWPE的加工性能并保持较好的力学性能,因而UHMWPE/PP共混体系的研究受到广泛关注。本文首先介绍了限制UHMWPE加工成型的主要原因,其次从相态结构、流动性能、力学性能及耐磨性能等方面综述了近年来UHMWPE/PP共混改性的研究进展,最后对其发展方向进行了展望。     

PP在熔融沉积成型工艺中的应用

选取不同结构的聚丙烯(PP),加入不同的填料或助剂、其他聚合物,用熔融沉积成型(FDM)打印机测试不同体系的打印性能,并对改性PP进行了力学性能测试。结果表明:收缩率是FDM打印工艺最重要的指标,收缩率在1%左右的PP,加入木粉、纳米碳酸钙、聚碳酸酯有利于降低收缩率,可改善打印产品的质量;对于收缩率较低的PP体系,纳米碳酸钙和石油树脂的协同作用不仅降低了PP的收缩率,还减弱了材料的各向异性;对于中试PP试样,纳米碳酸钙的改善作用不明显,单独加入石油树脂HPN-600ei后,改性PP的收缩率降低,并减弱了各向异性。     

改性聚丙烯材料收缩率的研究

以滑石粉为填料,乙烯-辛烯共聚物(POE)和聚乙烯作改性剂,研究了改性剂用量、注塑工艺及放置时间对改性聚丙烯(PP)收缩率的影响.结果表明,通过加入弹性体、滑石粉和聚乙烯可以大幅降低产品的收缩率,通过注塑成型工艺可以对成型制件的收缩率进行微调.     

SEBS/PP共混材料的研究及其进展

SEBS是一种用途广泛的新型弹性体材料,在常温下具有高弹性,高温下可直接加工成型。由于SEBS具有优异的耐臭氧、耐氧化、耐紫外线和耐候性能等,因此,应用范围广于普通SBS材料。但是,SEBS耐溶剂性和耐油性较差,常通过与其他材料共混改性来增强其加工性能。文章重点概述了苯乙烯-乙烯-丁烯-苯乙烯(SEBS)与聚丙烯(PP)共混材料的微观结构、相容性以及结构与性能的研究进展,介绍了近年国内外SEBS/PP共混改性的研究成果,包括填充油、无机材料、PPO、PC和PA6等改性体系,并比较了这些改性技术对SEBS/PP共混体系微观结构及性能的影响,近年内,SEBS/PP共混材料的理论研究和工程应用会有长足发展。     

功能化聚丙烯用作相容剂的研究

研究了功能化改性聚丙烯(PP)对PP/苯乙烯-丁二烯-苯乙烯三嵌段共聚物/有机蒙脱土共混体系结构和性能的影响。用X射线衍射仪、偏光显微镜和透射电子显微镜等分析了共混体系的结构与形貌。结果表明,接枝功能化聚丙烯(MPP)的加入,促进了PP的β晶型生成,减小了晶粒尺寸,改善了共混体系的相容性。在拉伸强度下降幅度较小的情况下,MPP的引入较明显地提高了共混体系的抗冲击性能和热性能。     

欧盟公布染料化学名称

该文根据欧盟2000年公布的第五版和2002年公布的第六版《欧洲化学物质申报清单》，选择一些重要的染料品种，介绍了他们的化学名称，以及可供参考的结构式。     

Effect of protein fusion on the transition temperature of an environmentally responsive elastin-like polypeptide: a role for surface hydrophobicity?

The limited throughput, scalability and high cost of protein purification by chromatography provide motivation for the development of non-chromatographic protein purification technologies that are cheaper and easier to implement in a high-throughput format for proteomics applications and to scale up for industrial bioprocessing. We have shown that genetic fusion of a recombinant protein to an elastin-like polypeptide (ELP) imparts the environmentally sensitive solubility property of the ELP to the fusion protein, and thereby allows selective separation of the fusion protein from Escherichia coli lysate by aggregation above a critical temperature (T(t)). Further development of ELP fusion proteins as widely applicable purification tools necessitates a quantitative understanding of how fused proteins perturb the ELP T(t) such that purification conditions (T(t)) may be predicted a priori for new recombinant proteins. We report here the effect that fusing six different proteins has on the T(t) of an ELP. A negative correlation between T(t) and the fraction hydrophobic surface area on the fused proteins was observed, which was determined from computer modeling of the available three-dimensional structure. The thermally triggered aggregation behavior of ELP-coated, functionalized gold colloids as well as ligand binding to the tendamistat-ELP fusion protein support the hypothesis that hydrophobic surfaces in molecular proximity to ELPs depress the ELP T(t) by a mechanism analogous to hydrophobic residue substitution in the ELP repeat, Val-Pro-Gly-Xaa-Gly.     

An efficient method for creation and functional analysis of libraries of hybrid type I polyketide synthases

Bacterial type I polyketide synthases (PKSs) generate a structurally diverse group of natural products with a wide range of biological activities. Hybrid type I PKSs in which domains of one multifunctional polypeptide are replaced with components from heterologous systems have generated significant interest over the past decade. Almost invariably only one or several specific hybrids are made at a time and tested for functionality. This approach is slow, dependent upon a fortuitous choice of specific fusions points, and often leads to inactive or minimally active hybrid systems. We describe herein a method for generating and screening a library of hybrid pikAI complementation plasmids (encoding the loading domain and the first two extension domains of pikromycin PKS) able to restore pikromycin in a BB138 Streptomyces venezuelae pikAI-deletion mutant. In the first step the plasmid sequence encoding the loading domain AT(0)-ACP(0) was replaced by a counter selectable marker, sacB. DNA family shuffling was then used to generate a diverse library of chimeric AT(0)-ACP(0) fragments, which were used to replace sacB by lambda-Red-mediated in vivo recombination in an Escherichia coli host. This method resulted in the rapid and efficient generation of a large number of hybrid pikAI complementation plasmids, which were used to transform S.venezuelae BB138. A bioassay of over 4000 of these transformants successfully revealed three different PikAI hybrids which were able to lead to pikromycin production. The study suggests that most of the hybrids are not detectably functional, and underscores the need to generate and screen large and diverse libraries in which different fusion points are tried. The methodologies applied in this study address this need and can be used for directed evolution of any component of the PikPKS, and potentially other type I PKS systems.     

A novel emulsion mixture for in vitro compartmentalization of transcription and translation in the rabbit reticulocyte system

Emulsion formulations used for in vitro compartmentalization (IVC) methods were found to be incompatible with protein expression in the rabbit reticulocyte (RRL) system, causing rapid discoloration and translation shutdown. Here we identify possible causes and describe a novel water-in-oil emulsion which abolished discoloration and allowed high-level in-emulsion expression of active luciferase and human telomerase using the RRL. This novel emulsion greatly expands the range of potential protein targets for IVC.     

Identification of potent human anti-IL-1RI antagonist antibodies

Interleukin-1 (IL-1) blockade by IL-1 receptor antagonist benefits some arthritis patients by reducing joint damage. This fact inspired us to develop antagonist human therapeutic antibodies against IL-1R(I) using phage libraries that display single-chain variable fragment (scFv) antibody fragments. Panning libraries against human IL-1R(I) generated 39 unique scFv-phage whose binding to IL-1R(I) was competed by IL-1 ligands. Fifteen of these scFv-phage, identified using IL-1R(I)-binding assays and dissociation rate ranking, were reformatted as scFv-Fc and IgG(4) molecules. The ease of producing antibodies in the scFv-Fc format permitted rapid identification of four lead clones (C10, C13, C14, C15) that inhibit NF-kappaB nuclear translocation induced by IL-1. Reformatting these clones as IgG(4) molecules increased their inhibition potency by 相似文献   

Conservation and covariance in PH domain sequences: physicochemical profile and information theoretical analysis of XLA-causing mutations in the Btk PH domain

Mutations that cause X-linked agammaglobulinemia (XLA) appear throughout the Bruton tyrosine kinase (Btk) sequence, including the pleckstrin homology (PH) domain. To analyze the basis of this disease with respect to protein structure, we studied the relationships between PH domain sequences and structures by comparing sequence-based profiles of physicochemical properties and solvent accessibility profiles. The diversity of the distribution of amino acids was measured by calculating entropies for sequences containing mutations at different positions in multiple sequence alignments. Mutual information was calculated to quantify positional covariation. Eight conserved extrema were apparent in all profiles. The majority of the XLA disease-causing mutations in the Btk PH domain were found at positions having significant mutual information, indicating that there are covariant constraints for both structure and function. Together with additional structural analyses, all the XLA mutations that were analyzed could be explained at the molecular level. The method developed here is applicable to the design of mutations for protein engineering.     

Improved activity and thermostability of Candida antarctica lipase B by DNA family shuffling

DNA family shuffling was used to create chimeric lipase B proteins with improved activity toward the hydrolysis of diethyl 3-(3',4'-dichlorophenyl)glutarate (DDG). Three homologous lipases from Candida antarctica ATCC 32657, Hyphozyma sp. CBS 648.91 and Crytococcus tsukubaensis ATCC 24555 were cloned and shuffled to generate a diverse gene library. A high-throughput screening assay was developed and used successfully to identify chimeric lipase B proteins having a 20-fold higher activity toward DDG than lipase B from C.antarctica ATCC 32657 and a 13-fold higher activity than the most active parent derived from C.tsukubaensis ATCC 24555. In addition, the stability characteristics of several highly active chimeric proteins were also improved as a result of family shuffling. For example, the half-life at 45 degrees C and melting point (T(m)) of one chimera exceeded those of lipase B from C.antarctica ATCC 32657 by 11-fold and 6.4 degrees C, respectively, which closely approached the stability characteristics of the most thermostable parent derived from Hyphozyma sp. CBS 648.91.     

Improvement of cyclodextrin glucanotransferase as an antistaling enzyme by error-prone PCR

In an effort to improve the properties of cyclodextrin glucanotransferase (CGTase) as an antistaling enzyme, error-prone PCR was used to introduce random mutations into a CGTase cloned from alkalophilic Bacillus sp. I-5 (CGTase I-5). A mutant CGTase[3-18] with the three mutations M234T, F259I and V591A was selected by agar plate assay. Sequence alignment of various CGTases indicated that M234 and F259 are located in the vicinity of the catalytic sites of the enzyme and V591 in the starch binding domain E. The cyclization activity of CGTase[3-18] was dramatically decreased by 10-fold, while the hydrolyzing activity was increased by up to 15-fold. These mutations near subsite +1 (M234T) and at subsite +2 (F259I) are likely to alter the enzyme activity in a concerted manner, promoting hydrolysis of substrate while retarding cyclization. The addition of CGTase[3-18] reduced the retrogradation rate of bread by as much as did the commercial antistaling enzyme Novamyl during 7-day storage at 4 degrees C. No cyclodextrin (CD) was detected in bread treated with CGTase[3-18], whereas 21 mg of CD per 10 g of bread was produced in bread treated with wild-type CGTase.     

Fusion of the antiferritin antibody VL domain to barnase results in enhanced solubility and altered pH stability

Chimeric immunotoxins that combine antigen recognition domains of antibodies and cytotoxic RNases have attracted much attention in recent years as potential targeted agents for cancer immunotherapy. In an attempt to obtain a structurally minimized immunofusion for folding/stability studies, we constructed the chimeric protein VL-barnase. The chimera comprises a small cytotoxic enzyme barnase, ribonuclease from Bacillus amyloliquefaciens, fused to the C-terminus of the light chain variable domain (VL) of the anti-human ferritin monoclonal antibody F11. While the individual VL domain was expressed in Escherichia coli as insoluble protein packed into inclusion bodies, its fusion to barnase resulted in a significant ( approximately 70%) fraction of soluble protein, with only a minor insoluble fraction ( approximately 30%) packed into inclusion bodies. The in vivo solubilizing effect of barnase was also observed in vitro and suggests a chaperone-like role that barnase exerted with regard to the N-terminal VL domain. Cytoplasmic VL-barnase was analyzed for structural and functional properties. The dimeric state of the chimeric protein was demonstrated by size-exclusion chromatography, thus indicating that fusion to barnase did not abrogate the intrinsic dimerization propensity of the VL domain. Ferritin-binding affinity and specificity in terms of constants of association with isoferritins were identical for the isolated VL domain and its barnase fusion, and RNase activity remained unchanged after the fusion. Intrinsic fluorescence spectra showed a fully compact tertiary structure of the fusion protein. However, significantly altered pH stability of the fusion protein versus individual VL and barnase was shown by the pH-induced changes in both intrinsic fluorescence and binding of ANS. Together, the results indicate that VL-barnase retained the antigen-binding affinity, specificity and RNase activity pertinent to the two individual constituents, and that their fusion into a single-chain chimeric protein resulted in an altered tertiary fold and pH stability.     

A cell-based screen for function of the four-helix bundle protein Rop: a new tool for combinatorial experiments in biophysics

Combinatorial methodologies have revolutionized studies in biomolecular function, but they have so far proven less useful for understanding macromolecular structure and stability. This is largely because of the difficulty of screening libraries of molecules for biophysical properties, and the difficulty of interpreting structural effects in complicated molecules. Here, we report a novel, robust, cell-based screen for function of the four-helix bundle protein, Rop. By expression of green fluorescent protein from a ColE1 plasmid, the screen reports the copy number of the plasmid, which is modulated in Escherichia coli by Rop. We have engineered the screen so that the fluorescent phenotype can correspond to either Rop activity or lack thereof. We have used the screen to demonstrate with systematically constructed Rop core variants that not all molecules that bind small stem-loop RNAs in vitro are active in vivo. Rop is well understood from structural work and systematic mutations, which makes it possible to construct rational, targeted libraries. This screen makes it possible to rapidly interrogate such libraries effectively for proper protein folding and stability. In addition to its intended utility for combinatorial experiments in biophysics, the screen will allow further dissection of the mechanism of Rop-mediated plasmid copy number regulation in vivo.