26908-94-1Relevant articles and documents
Immunomodulatory peptides
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, (2014/12/12)
The invention relates to peptides derivatized with a hydrophilic polymer which, in some embodiments, bind to human FcRn and inhibit binding of the Fc portion of an IgG to an FcRn, thereby modulating serum IgG levels. The disclosed compositions and methods may be used in some embodiments, for example, in treating autoimmune diseases and inflammatory disorders. The invention also relates, in further embodiments, to methods of using and methods of making the peptides of the invention.
Process for producing alpha 2,3/ alpha 2,8-sialyltransferase and sialic acid-containing complex sugar
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, (2008/06/13)
The present invention can provide a process for producing a protein having α2,3/α2,8-sialyltransferase activity using a transformant comprising a DNA encoding a protein having α2,3/α2,8-sialyltransferase activity derived from a microorganism belonging to the genus Pasteurella and a process for producing a sialic acid-containing complex carbohydrate using a transformant capable of producing a protein having α2,3/α2,8-sialyltransferase activity derived from a microorganism.
Hydrogels from biopolymers
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, (2008/06/13)
Methods are disclosed for preparing linear or/and partial precross-linked poly-g-glutamic acid nanoparticle products, their reaction with compounds which contain vinyl groups, and the polymerization by chemical initiation or photopolymerization of these by light of predetermined wavelength. The final products of the present invention are useful as local drug delivery systems, dental surgery, and for inhibition of post-surgical adhesion. The hydrogels made from the biopolymers of the present invention may also be used in controlled release devices, superabsorbent materials and biomaterials like enzyme immobilization.
Gene recombinant antibody and antibody fragment thereof
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, (2008/06/13)
A recombinant antibody or the antibody fragment thereof which specifically reacts with an extracellular domain of human CCR4; a DNA which encodes the recombinant antibody or the antibody fragment thereof; a method for producing the recombinant antibody or the antibody fragment thereof; a method for immunologically detecting CCR4, a method for immunologically detecting a cell which expressed CCR4 on the cell surface, a method for depleting a cell which expresses CCR4 on the cell surface, and a method for inhibiting production of Th2 cytokine, which comprise using the recombinant antibody according or antibody fragment thereof; a therapeutic or diagnostic agent for Th2-mediated immune diseases; and a therapeutic or diagnostic agent for a blood cancer.
Peptides with an insulin-like action
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, (2008/06/13)
Peptides with an insulin-like action, of formula I: STR1 in which G is a hydrogen atom, an amino add residue, or a monosubstituted or polysubstituted amino acid; D is an amino acid residue, a phosphoamino acid residue, a monosaccharide residue, or a covalent bond; E is --NH--(CH2)n --NR52, a glycerol residue, or --NH--(CH2)p --R6 --R7 ; R1 is (C1 -C4)-alkyl or =O; R2 is a sulfhydryl protecting group, (C1 -C3)-alkyl, or a hydrogen atom; R3 and R4, independently of one another, are a hydrogen atom or methyl; R5, each being identical or different, is a hydrogen atom, 1 to 6 monosaccharide residues, or 1 to 6 monosubstituted or polysubstituted monosaccharide residues; R6 is O PO4 H, PO2 H, NHCOO, S or OCOO; R7 is a hydrogen atom, 1 to 6 monosaccharide residues, or 1 to 6 monosubstituted or polysubstituted monosaccharide residues; w is an integer 1 or 2; their preparation and use for treatment of diabetes mellitus or insulin-independent diabetes.
Novel cyclic Hexapeptide LHRH antagonists
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, (2008/06/13)
Novel peptides of the formula: STR1 where R 1 through R 8 are various radicals derived from L- and D- amino acids; having LHRH antagonist activity; useful in reducing fertility.Pharmaceutical compositions and methods for use in reducing fertility.
Conversion of Aliphatic Amides into Amines with benzene. Scope of the Reaction
Loudon, G. Marc,Radhakrishna, A. S.,Almond, Merrick R.,Blodgett, James K.,Boutin, Raymond H.
, p. 4272 - 4276 (2007/10/02)
The reagent benzene, PIFA, brings about the facile oxidative rearrangement of aliphatic amides to amines in mildly acidic (pH 1-3) mixed aqueous-organic solvents.Aromatic amines are further oxidized by the reagent and therefore cannot be prepared by this method.The rearrangement, which is in effect an "Hofmann rearrangement", occurs with complete retention of configuration in the migrating group, and the rate of the reaction follows approximately the migratory aptitudes of the migrating groups determined for other similar reactions.Isocyanates are intermediates in the rearrangement but are rapidly hydrolyzed to the product amines under the mildly acidic conditions.The acidic conditions protect the product amines from reacting with the isocyanate intermediates and forming ureas.The reaction is accelerated by addition of pyridine to a pH of approximately 3.The scope of the reaction is discussed.
Critical Examination of a Method for the Analysis of α and ω Linkages in Peptides Containing Aspartic Acid and Glutamic Acid
Capecchi, John T.,Miller, Marvin, J.,Loudon, G. Marc
, p. 2014 - 2021 (2007/10/02)
Coupling of O-pivaloylhydroxylamine (4) and subsequent Lossen rearrangement under mild conditions led to the disappearence of β-aspartyl and γ-glutamyl residues from subsequent amino acid analysis in a variety of peptides.Residues from the usual α linkage rearrange much more sluggishly to products that are detectable by amino acid analysis.An interesting complication in the procedure is that α-linked glutamyl residues are converted in part to a 2-oxohexahydropyrimidine-4-carboxylic acid derivative which is stable to extended acid hydrolysis.After base hydrolysis this deri vative yields 2,4-diaminobutanoic acid.This reaction explains aberrant results in the linkage analysis of collagen that have been reported in the literature.
Vancomycin: Structure and Transformation to CDP-I
Harris, Constance M.,Kopecka, Hana,Harris, Thomas M.
, p. 6915 - 6922 (2007/10/02)
The structure of vancomycin is assigned as 7 in which aspartate is present as asparagine, rather than isoasparagine (i.e., 4) as had been proposed previously (Williamson, M.P.; Williams, D.H.J.Am.Chem.Soc. 1981, 103, 6580).The mechanism of rearrangement of vancomycin to CDP-I has been investigated.The pathway is deduced: vancomycin -> succinimide 11 -> CDP-I-m (3) CDP-I-M (2).Succinimide 11 has been isolated and characterized by FT-IR and FAB-MS; these data are in agreement with an in-chain succinimide but not a seco structure.Treatment of 11 at pH 8 leads to immediate appearance of the minor form of CDP-I, which slowly yields an equilibrium mixture with the major form (ca. 64:36 of 2:3).No major change in the equilibrium ratio or rate of equilibration was found by changing solvent (H2O, Me2SO, or 0.1percent TFA/20percent 2-propanol) or pH (in the range 2.0-8.0).High-field 1H NMR studies of 2 and 3 indicate that they are atropisomers involving different orientations of the Cl-substituted aromatic ring of residue 2, in agreement with earlier assignments by Williamson and Williams.It is concluded that 2 and 3 can interconvert by simple reorientation of the aromatic ring rather than via a transient cleavage product.The cyclophane ring in which the Cl-substituted aromatic residue 2 is embedded is enlarged by one methylene unit in the conversion of vancomycin to CDP-I; rotation of ring 2 can occur in CDP-I but not in vancomycin.The additional methylene unit in the N-terminal cyclophane ring of CDP-I causes the ring to lie in a conformation that is significantly different from that of vancomycin.