1,721,043 research outputs found
Sistemi Bifenillici Flessibili come Sonde per la Determinazione della Configurazione Assoluta di 1,2- e 1,3-Dioli Mediante Spettroscopia DC
No full textTumor Necrosis Factor-a Neutralizing Antibodies Induced by a Glycolaldehyde-Modified C- terminal Polypeptide.
No full textTNF-a is a pro-inflammatory cytokine that is overexpressed in diverse inflammatory states such as rheumatoid arthritis. Anti-TNF therapies, including monoclonal antibodies (Abs), have demonstrated remarkable success in management of arthritis and other chronic inflammatory diseases. The possibility to elicit autoAbs to TNF-a (beneficial autoimmunity) has been proposed as an immunotherapeutic approach to neutralize systemic TNF-a (1). Studies using a DNA vaccination strategy in rat adjuvant arthritis mapped several epitopes for natural anti-TNF-a autoAbs in the C-terminal portion of the sequence. We previously showed that aldehyde-tagged peptide conjugates representing immunogenic epitopes of toxic shock syndrome toxin–1, could induce anti-toxin neutralizing Abs without the need of potent adjuvants (2). In the present study, using a C-terminal TNF-a recombinant polypeptide, we followed a similar approach to generate neutralizing Abs against TNF-a in Lewis rats. Immunized rats showed less severe symptoms in the collagen induced arthritis ( CIA) model.
1. Dalum I. et. al. Therapeutic antibodies elicited by immunization against TNF-alpha. Nat Biotechnol 1999. 17:666-669.
2. Bavoso A, Ostuni A, De Vendel J, Pollaro F, Armentano F, Knight T, Makker S. and A. Tramontano. Aldehyde modification of peptide immunogen enhances protein-reactive antibody response to toxic shock syndrome toxin-1. J Pept Sci 2006. 12:843-849
Flexible Biphenyls as Probes for the Determination of Absolute Configuration of 1,2- and 1,3-Diols by CD Spectroscopy
No full textCoordination of 2-hydroxyhippuric acid to the copper(II) ion: A solution and solid state study
No full text
Flexible Biphenyls as Probes for Configurational Assignment of 1,2- and 1,3-Diols by CD Spectroscopy
No full textAntioxidant potential of the polyherbal formulation “ImmuPlus”, a nutritional supplement for horses
No full textIn order to counteract harmful effects of oxidative stress due to pathological conditions or physical exercise, horses are often
administered dietary supplements having supposed high antioxidant activities. The aim of the present study was to identify the
in vitro antioxidant potential of “ImmuPlus”, a polyherbal formulation (Global Herbs LTD, Chichester,West Sussex, Great Britain),
containing three medicinal plants (Withania somnifera, Tinospora cordifolia, and Emblica officinalis), known in Ayurveda for their
use in human disease treatment. Extracts obtained by different solvents (water,methanol, ethanol, acetone, and hexane) were tested
for total antioxidant capacity, total reducing power, scavenging activity against DPPH radical, and total polyphenol and flavonoid
contents. Our results showed that, except as regards hexane, all the used solvents are able to extract compounds having high
antioxidant activity, even when compared to ascorbic acid. Regression analysis showed significant correlations between antioxidant
properties and polyphenol/flavonoid contents, indicating the latter, known for their beneficial effects on health of human and animal
beings, as major components responsible for the strong antioxidant capacities.Moreover, obtained results suggest the effective role
of the polyherbal mixture as good source of antioxidants in horses
Formation, crystal structure and coordination chemistry of Mn(III)(eospz)(SH) [oespz(2-)] =2,3,7,8,12,13,17,28-octakis(ethylsupfanyl)-5,10,15,20-tetraazaporphyrinate dianion] complexe
No full textReaction of [Mn(oespz)] [oespz(2-) = 2,3,7,8,12,13,17, 18-octakis(ethylsulfanyl)-5, IO, 15,20-tetraazaporphyrinate dianion (porphyrazinate)] with CS, and, subsequently, with THF, afforded the hydrogensulfido(1 -)manganese(Iu) ethylsulfanylporphyrazinate [ln(oespz)(SK)], in high yield. The S-H stretching absorptions are not observed in the IR spectrum of the complex, whereas a peak at delta 10.3 (vs. SiMe4) ascribed to the hydrogensulfido proton resonance, is observed in the H-1 NMR spectrum. The complex was shown to be isostructural with [M(oespz)Cl] (M = Fe or Mn) by X-ray crystallography. The crystal packing of the complex consists of slipped stacks of dimeric units with the monomers positioned in a trans fashion with respect to the Mn-S-apical bond. Magnetic data are consistent with weakly antiferromagnetically coupled high spin (S = 2) manganese(III) centers. A possible pathway to the oxidative addition of CS, to the manganese(II) center has been proposed. In CHCl3 [Mn(oespz)(SH)] reacts reversibly through the axial hydrosulfido ligand with the sterically hindered base 2,4,6-trimethylpyridine, whereas the complex co-ordinates 1-methylimidazole reversibly on the vacant site of manganese. Treatment of the complex with 1-methylimidazole in benzene leads to a Mn-III-Mn-II redox process, as deduced from the UV/VIS spectra
Crystal structure of high-spin (S= 5/2) manganese(II) 2,3,7,8,12,13,17,18-octakis (ethylsulfanyl)-5,10,15,20-tetraazaporphyrinate
No full textStructural features in EIAV NCp11: a lentivirus nucleocapsid protein with a short linker.
No full textLentiviral nucleocapsid proteins are a class of multifunctional proteins that play an essential role in RNA packaging and viral infectivity. They contain two CX2CX4HX4C zinc binding motifs connected by a basic linker of variable length. The 3D structure of a 37-aa peptide corresponding to sequence 22-
58 from lentiviral EIAV nucleocapsid protein NCp11, complexed with zinc, has been determined by 2D
1H NMR spectroscopy, simulated annealing, and molecular dynamics. The solution structure consists of
two zinc binding domains held together by a five-residue basic linker Arg38-Ala-Pro-Lys-Val42
that allows for spatial proximity between the two finger domains. Observed linker folding is stabilized by H bonded secondary structure elements, resulting in an omega-shaped central region, asymmetrically centered on the linker. The conformational differences and similarities with other NC zinc binding knuckles have been
systematically analyzed. The two CCHC motifs, both characterized by a peculiar Pro-Gly sequence
preceding the His residue, although preserving Zn-binding geometry and chirality of other known NC
proteins, exhibit local fold differences both between each other and in comparison with other previously
characterized retroviral CCHC motifs
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