1,720,978 research outputs found
Inclusion of diprotonated [2.2.2]cryptand in the cavity of uranyl-complexed p-phenyltetrahomodioxacalix[4]arene
No full textCsF-Promoted acetyl dance at the narrow rim of p-tert-Butyl[3.1.3.1]homooxacalixarene” Org. Lett. 2006, 8, 4405-4408
No full text5,5’-Di-tert-butyl-2,2’-dihydroxy-3,3'-methylenedibenzaldehyde and 6,6’-di-tert-butyl-8,8’-methylenebis(spiro[4H-1,3-benzodioxin-2,1’-cyclohexane])
No full textMETHYL ETHER DERIVATIVES OF p-tert-BUTYL[3.1.3.1]HOMOOXACALIXARENE. FORMATION, STRUCTURE, AND COMPLEXES WITH QUATERNARY AMMONIUM IONS
No full textDesign of a bioinformatics algorithm for the assessment of mouse gut phylotypes identified by metaproteomic approach
No full textPerusal of food allergens analysis by mass spectrometry-based proteomics
No full textFood allergy is the disease where the immune system is elicited by antigens in food. Although innocuous for immune-tolerant individuals, an ever-growing number of food allergenic people are being registered worldwide. To date, no treatment to cure food allergy is available and the disease management relies on the careful exclusion of the allergenic food from the diet of the allergic individuals. Great efforts are ongoing to clarify the allergenic mechanisms of the diverse allergenic proteins of food origin, aimed to both designing suitable therapies and for a timely and precise diagnosis of the allergic condition. Among the other omics sciences, mass spectrometry (MS)-based proteomics is gaining a steadily increasing interest by the whole scientific community acknowledged its high versatility. In the present work, the latest proteomics based-studies on allergenic proteins are reviewed to provide guidance on the different MS-based methodologies adopted in the research on food allergens. Our review points to highlight the strengths of the MS-based proteomics and how these have been exploited to address specific research questions. Also, the most common drawbacks encountered in a proteomic study are discussed, providing an overview that helps novel researchers in choosing the more suitable experimental workflow. Significance: Wide wealth of knowledge arising from the various MS-based proteomic investigations is improving our understanding of food allergy through molecular characterization of food allergens. The present work reviews the key aspects to be evaluated while investigating food allergens by means of MS-based proteomics and provide guidance to the novel research groups approaching to the fascinating world of MS-based food allergens detection
Proteomic investigations on the effect of different membrane materials on blood protein adsorption during haemodialysis
No full textDuring haemodialysis procedure, the contact of blood with the membrane material contained in the hemodialyser results in protein deposition and adsorption, and surface-adsorbed proteins may trigger a variety of biological pathways with potential pathophysiologic consequences. The present work was undertaken to examine for protein adsorption capacity of two membranes used for clinical haemodialysis, namely cellulose triacetate (a derivatized cellulosic membrane) and the synthetic polymer polysulfone-based helixone
pH-regulated formation of side products in the reductive amination approach for differential labeling of peptides in relative quantitative experiments
Get PDFAmong the most common stable-isotope labeling strategies, the reaction of formaldehyde with peptides in the presence of NaCNBH₃ features many attractive aspects that are conducive to its employment in quantitation experiments in proteomics. Reductive amination, with formaldehyde and d(2)-formaldehyde, is reported to be a fast, easy, and specific reaction, undoubtedly inexpensive if compared with commercially available kits for differential isotope coding. Acetaldehyde and d(4)-acetaldehyde could be employed as well without a substantial increase in terms of cost, and should provide a wider spacing between the differentially tagged peptides in the mass spectrum. Nevertheless, only a single paper reports about a diethylation approach for quantitation. We undertook a systematic analytical investigation on the reductive amination of some standard peptides pointing out the occasional occurrence of side reactions in dependence of pH or reagents order of addition, particularly observing the formation of cyclic adducts ascribable to rearrangements involving the generated Schiff-base and all the nucleophilic sites of its chemical environment. We also tried to evaluate how much this side-products amount may impair isotope coded relative quantitation
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