80 research outputs found
Study of the anti-idiotypic resonse to anti-LA/SSB autoantibodies using complementary peptides to B- and T-cell epitopes of La/SSB
Induction of immune responses in inbreed mice by immunizations with the complementary 289-308 La/SSB epitope
17O NMR and FT-IR study of the ionization state of peptides in aprotic solvents Application to Leu-enkephalin
AbstractThe ionization state of Leu-enkephalin in DMSO and MeCN/DMSO (4/1) solution was studied by the combined use of 17O NMR and FT-IR spectroscopy. After lyophilization or an aqueous solution at nearly neutral pH, Leu-enkephalin essentially exists in the uncharged state in MeCN/DMSO (4/1) solution. In pure DMSO, only 40% of the Leu-enkephalin molecules are in the zwitterionic state under the same conditions
Antigenic role of single residues within the main immunogenic region of the nicotinic acetylcholine receptor
Optimization of relay placement and power allocation for decode-and-forward cooperative relaying over correlated shadowed fading channels
Development of a diagnostic immunoassay for the detection of natural anti-NTM/VIP antibodies of HIV-1
Development of a diagnostic immunoassay for the detection of natural anti-NTM/VIP antibodies of HIV-1
A diepitopic sequential oligopeptide carrier (SOCn) as mimic of the Sm autoantigen: Synthesis, conformation and biological assays
Anti-Sm (Sm: U1-U6 RNA-protein complex) antibodies are usually considered highly specific for systemic lupus erythematosus (SLE), while anti-U1RNP (U1RNP: U1RNA-protein complex) are thought of as diagnostic criteria for the mixed connective tissue disease (MCTD). However, both antibody specificities coexist in SLE and MCTD, in varying percentages. Although the anti-Sm/anti-U1RNP immunological cross-reactivity has been initially attributed to a common motif, PPXY(Z)PP (where X, Y, Z are various amino acids), found in the Sm, U1-A and U1-C autoantigens, it appears that the conformational features of the Sm epitopes also play an important role in the immunoreactivity. The PPGMRPP and PPGIRGP main epitopes of the Sm antigen were coupled in duplicate to the tetrameric Ac-(Lys-Aib-Gly)4-OH, SOC4, carrier to form the [(PPGMRPP)2, (PPGIRGP)2]-SOC4 construct as a mimic of the native Sm. It was found that: (i) the 310 helical structure of SOC4 allows the epitopes to adopt an exposed orientation, similar to their free forms, that facilitates their recognition from the anti-Sm antibodies, and (ii) the U1-RNP cross-reactivity is minimized. Copyright © 2001 European Peptide Society and John Wiley & Sons, Ltd
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