Your browser doesn't support javascript.
loading
Mostrar: 20 | 50 | 100
Resultados 1 - 16 de 16
Filtrar
Mais filtros








Base de dados
Intervalo de ano de publicação
1.
Acta Naturae ; 14(2): 85-92, 2022.
Artigo em Inglês | MEDLINE | ID: mdl-35923565

RESUMO

Previous studies have shown that in the blood of healthy donors (1) there are no natural antibodies against sialylated glycoproteins, which contain Neu5Acα (N-acetylneuraminic acid) as the most widespread form of human sialic acid, and (2) there is a moderate level of antibodies capable of binding unnatural oligosaccharides, where Neu5Ac is beta-linked to a typical mammalian glycan core. In the present study, we investigated antibodies against ßNeu5Ac in more detail and verified the presence of Kdn (2-keto-3-deoxy- D-glycero-D-galacto-nonulosonic acid) as a possible cause behind their appearance in humans, taking into account the expected cross-reactivity to Kdn glycans, which are found in bacterial glycoconjugates in both the α- and ß-forms. We observed the binding of peripheral blood immunoglobulins to sialyllactosamines (where "sialyl" is Kdn or neuraminic acid) in only a very limited number of donors, while the binding to monosaccharide Kdn occurred in all samples, regardless of the configuration of the glycosidic bond of the Kdn moiety. In some individuals, the binding level of some of the immunoglobulins was high. This means that bacterial Kdn glycoconjugates are very unlikely to induce antibodies to ßNeu5Ac glycans in humans. To determine the reason for the presence of these antibodies, we focused on noninfectious pathologies, as well as on a normal state in which a significant change in the immune system occurs: namely, pregnancy. As a result, we found that 2/3 of pregnant women have IgM in the blood against Neu5Acß2-3Galß1-4GlcNAcß. Moreover, IgG class antibodies against Neu5Acß2-3Galß1-4GlcNAcß and Neu5Acß2-6Galß1-4GlcNAcß were also detected in eluates from the placenta. Presumably, these antibodies block fetal antigens.

2.
Biochemistry (Mosc) ; 84(10): 1177-1185, 2019 Oct.
Artigo em Inglês | MEDLINE | ID: mdl-31694513

RESUMO

It was previously shown that hemagglutinin residues Thr155, Glu158, and Ser228 are crucial for the recognition of Neu5Gc. In this study, we demonstrated that the ability to bind the Neu5Gc-terminated receptor is related to the amino acid 145: viruses of years 1972-1999 with Lys145 bind to the receptor, whereas viruses with Asn145 do not. Sporadic appearance and disappearance of the ability to bind Neu5Gc oligosaccharides and the absence of Neu5Gc in the composition of human glycoconjugates indicate the non-adaptive nature of this ability. It was previously shown that unlike H1N1 viruses, H3N2 viruses of years 1968-1989 did not distinguish between Neu5Acα2-6Galß1-4Glc (6'SL) and Neu5Acα2-6Galß1-4GlcNAc (6'SLN). H3N2 viruses isolated after 1993 have acquired the ability to distinguish between 6'SL and 6'SLN, similarly to H1N1 viruses. We found that the affinity for 6'SLN has gradually increased from 1992 to 2003. After 2003, the viruses lost the ability to bind a number of sialosides, including 6'SL, that were good receptors for earlier H3N2 viruses, and retained high affinity for 6'SLN only, which correlated with the acquisition of new glycosylation sites at positions 122, 133, and 144, as well as Glu190Asp and Gly225Asp substitutions, in hemagglutinin. These substitutions are also responsible for the receptor-binding phenotype of human H1N1 viruses. We conclude that the convergent evolution of the receptor specificity of the H1N1 and H3N2 viruses indicates that 6'SLN is the optimal natural human receptor for influenza viruses.


Assuntos
Vírus da Influenza A Subtipo H3N2/química , Receptores Virais/química , Sítios de Ligação , Humanos , Vírus da Influenza A Subtipo H3N2/genética , Vírus da Influenza A Subtipo H3N2/metabolismo , Receptores Virais/sangue
3.
Bioorg Khim ; 41(2): 170-84, 2015.
Artigo em Russo | MEDLINE | ID: mdl-26165124

RESUMO

Synthesis of oligocaccharides Galß1-3GlcNAcß-sp, GlcNAcß1-3Galß1-3GlcNAcß-sp, Galß1-3GlcNAcß1-3Galß1-3GlcNAcß-sp, Galß1-3GlcNAcß1-3Galß1-4GlcNAcß-sp, Galß1-3GlcNAcß1-6Galß1-4GlcNAcß-sp (sp = O(CH2)3NH2 or O(CH2)2NH2) was carried out using glycosylation by N-Troc-protected derivatives of glycosamine or disaccharide Galß1-3GlcN.


Assuntos
Oligossacarídeos/química , Oligossacarídeos/síntese química , Configuração de Carboidratos
4.
Biochemistry (Mosc) ; 76(10): 1185-92, 2011 Oct.
Artigo em Inglês | MEDLINE | ID: mdl-22098245

RESUMO

The network of adhesion/growth-regulatory galectins in chicken (chicken galectin, CG) has only one tandem-repeat-type protein, CG8. Using a cell-based assay and probing galectin reactivity with a panel of fluorescent neoglycoconjugates (glycoprobes), its glycan-binding profile was determined. For internal validation, human galectin-8 (HG8) was tested. In comparison to HG8, CG8 showed a rather similar specificity: both galectins displayed high affinity to blood group ABH antigens as well as to 3'-sialylated and 3'-sulfated lactosamine chains. The most remarkable difference was found to be an ability of HG8 (but not CG8) to bind the disaccharide Galß1-3GlcNAc (Le(c)) as well as branched and linear oligolactosamines. The glycan-binding profile was shown to be influenced by glycocalix of the cell, where the galectin is anchored. Particularly, glycosidase treatment of galectin-loaded cells led to the change of the profile. Thus, we suppose the involvement of cis-glycans in the interaction of cell-anchored galectins with external glycoconjugates.


Assuntos
Antígenos de Grupos Sanguíneos/química , Dissacaridases/química , Galectinas/química , Galectinas/metabolismo , Animais , Antígenos de Grupos Sanguíneos/metabolismo , Linhagem Celular , Galinhas , Dissacaridases/metabolismo , Cães , Humanos , Rim/citologia , Estrutura Molecular , Polissacarídeos/química , Sequências de Repetição em Tandem
5.
Biochemistry (Mosc) ; 75(3): 310-9, 2010 Mar.
Artigo em Inglês | MEDLINE | ID: mdl-20370609

RESUMO

We have recently shown that the carbohydrate-binding pattern of galectins in cells differs from that determined in artificial (non-cellular) test-systems. To understand the observed discrepancy, we compared several test-systems differing in the mode of galectin presentation on solid phase. The most representative system was an assay where the binding of galectin (human galectins-1 and -3 were studied) to asialofetuin immobilized on solid phase was inhibited by polyacrylamide glycoconjugates, Glyc-PAA. This approach permits us to range quantitatively glycans (Glyc) by their affinity to galectin, i.e. to study both high and low affinity ligands. Our attempts to imitate the cell system by solid-phase assay were not successful. In the cell system galectin binds glycoconjugates by one carbohydrate-recognizing domain (CRD), and after that the binding to the remaining non-bound CRD is studied by means of fluorescein-labeled Glyc-PAA. In an "imitation" variant when galectins are loaded on adsorbed asialofetuin or Glyc-PAA followed by revealing of binding by the second Glyc-PAA, the interaction was not observed or glycans were ordered poorly, unlike in the inhibitory assay. When galectins were adsorbed on corresponding antibodies (when all CRDs were free for recognition by carbohydrate), a good concentration dependence was observed and patterns of specificities were similar (though not identical) for the two methods; notably, this system does not reflect the situation in the cell. Besides the above-mentioned, other variants of solid-phase analysis of galectin specificity were tested. The results elucidate the mechanism and consequence of galectin CRD cis-masking on cell surface.


Assuntos
Carboidratos/química , Galectinas/química , Sítios de Ligação
6.
Bioorg Khim ; 33(1): 131-47, 2007.
Artigo em Russo | MEDLINE | ID: mdl-17375668

RESUMO

The following spacered oligosaccharides were synthesized: GlcNAcbetal-3Galbetal-4GlcNAcbeta-sp, GlcNAcbetal-6Galbeta1-4GlcNAcbeta -sp, GlcNAcbeta -3(GlcNAcbeta1-6)Galbeta-4GllcNAcbeta-sp, Galbeta1-4GlcNAcbeta1-3Galbeta1-4GlcNAcbeta-sp, Galbeta1-4GlcNAcbetal-6Galbetal-4GlcNAcbeta-sp, Galbeta1-4GlcNAcbeta -3(Galbeta1-4GlcNAcbeta 1-6)Galbeta1-4GlcNAcbeta-sp, GlcNAcbeta1-3(Galbeta1-4GlcNAcbetal-6)Galbeta 1-4GlcNAcbeta-sp, and Galbeta1-4GlcNAcbetal-3(GlcNAcbetal-6)Galbetal-4GlcNAcbeta-sp (sp = O(CH2)2NH2). They represent N-acetyllactosamines substituted with N-acetylgly-cosamine or N-acetyllalctosamine residue at 03, O6, or at both positions of galactose. Glycosylation was achieved by coupling with N-trichloroethoxycarbonyl-protected glucosamine bromide in the presence of silver triflate.


Assuntos
Amino Açúcares/análise , Galectinas/química , Oligossacarídeos/química , Sequência de Carboidratos , Ligantes , Dados de Sequência Molecular , Oligossacarídeos/síntese química
7.
Vopr Virusol ; 51(4): 24-32, 2006.
Artigo em Russo | MEDLINE | ID: mdl-16929595

RESUMO

The ability of influenza viruses from different hosts to bind to the intestinal epithelium of various birds (Anseriformes (Anatidae), Galliformes, Charadriiformes (sandpipers and sea gulls), Ciconiiformes (storks), Podicipediformes (grebes), and Gruiformes was studied. The composition of sialo-containing receptors on the epithelia was examined, by using lectins. Intestinal epitheliocytes of the Anatidae (Anseriformes) family was shown to have a low content of receptors binding both Sambucus nigra agglutinin (SNA) lectin specific to Siaalpha-6Gal, and Maackia amurensis agglutinin (MAA) lection specific to Siaalpha2-2Gal. Nevertheless, these cells well bound duck influenza viruses. The intestinal epithelium of Ciconiiformes, Podicipediformes, and Gruiformes well bound MMA lection, but avian influenza viruses weakly bound the latter. The intestinal cells of Gallinaceae bound both MMA and SNA lectins and avian and human influenza viruses. Thus, the composition of natural sialosides is different in various avian species whereas the receptor specificity of influenza viruses from various hosts reflects these differences. This can be accounted for by the differences in the ability of influenza viruses from different birds to break through the interspecies barrier, infecting mammals and human beings in particular.


Assuntos
Aves , Vírus da Influenza A/fisiologia , Influenza Aviária/virologia , Mucosa Intestinal/química , Mucosa Intestinal/metabolismo , Mucinas , Oligossacarídeos , Receptores Virais/química , Receptores Virais/metabolismo , Mucosa Respiratória/química , Mucosa Respiratória/metabolismo , Animais , Aves/classificação , Aves/virologia , Humanos , Lectinas , Macaca , Modelos Moleculares , Mucinas/análise , Oligossacarídeos/análise , Oligossacarídeos/metabolismo , Especificidade da Espécie
8.
Biochemistry (Mosc) ; 71(5): 496-504, 2006 May.
Artigo em Inglês | MEDLINE | ID: mdl-16732727

RESUMO

Soluble siglecs-1, -4, -5, -6, -7, -8, -9, and -10 were probed with polyacrylamide glycoconjugates in which: 1) the Neu5Ac residue was substituted by a sulfate group (Su); 2) glycoconjugates contained both Su and Neu5Ac; 3) sialoglycoconjugates contained a tyrosine-O-sulfate residue. It was shown that sulfate derivatives of LacNAc did not bind siglecs-1, -4, -5, -6, -7, -8, -9, and -10; binding of 6'-O-Su-LacNAc to siglec-8 was stronger than binding of 3'SiaLacNAc. The relative affinity of 3'-O-Su-TF binding to siglecs-1, -4, and -8 was similar to that of 3'SiaTF. 3'-O-Su-Le(c) displayed two-fold weaker binding to siglec-1 and siglec-4 than 3'SiaLe(c). The interaction of soluble siglecs with sulfated oligosaccharides containing sialic acid was also studied. It was shown that siglecs-1, -4, -5, -6, -7, -9, and -10 did not interact with these compounds; binding of 6-O-Su-3'SiaLacNAc and 6-O-Su-3'SiaTF to siglec-8 was weaker than that of the corresponding sulfate-free sialoside probes. Siglec-8 displayed affinity to 6'-O-Su-LacNAc and 6'-O-Su-SiaLe(x), and defucosylation of the latter compound led to an increase in the binding. Sialoside probes containing tyrosine-O-sulfate residue did not display increased affinity to siglecs-1 and -5 compared with glycoconjugates containing only sialoside. Cell-bound siglecs-1, -5, -7, and -9 did not interact with 6-O-Su-3'SiaLacNAc, whereas the sulfate-free probe 3'SiaLacNAc demonstrated binding. In contrast, the presence of sulfate in 6-O-Su-6'SiaLacNAc did not affect binding of the sialoside probe to siglecs. 6'-O-Su-SiaLe(x) displayed affinity to cell-bound siglecs-1 and -5; its isomer 6-O-Su-SiaLe(x) bound more strongly to siglecs-1, -5, and -9 than SiaLe(x).


Assuntos
Lectinas/metabolismo , Oligossacarídeos/química , Sulfatos/química , Animais , Antígenos CD/genética , Antígenos CD/metabolismo , Antígenos de Diferenciação Mielomonocítica/genética , Antígenos de Diferenciação Mielomonocítica/metabolismo , Células CHO , Sequência de Carboidratos , Cricetinae , Cricetulus , Glicoconjugados/química , Glicoconjugados/farmacologia , Humanos , Lectinas/antagonistas & inibidores , Lectinas/genética , Glicoproteínas de Membrana/antagonistas & inibidores , Camundongos , Receptores Imunológicos/antagonistas & inibidores , Lectina 1 Semelhante a Ig de Ligação ao Ácido Siálico , Lectinas Semelhantes a Imunoglobulina de Ligação ao Ácido Siálico , Ácidos Siálicos/metabolismo , Especificidade por Substrato , Tirosina/análogos & derivados , Tirosina/química , Tirosina/metabolismo
9.
Antiviral Res ; 68(3): 116-23, 2005 Dec.
Artigo em Inglês | MEDLINE | ID: mdl-16214231

RESUMO

To develop a mouse model for testing receptor attachment inhibitors of human influenza viruses, the human clinical virus isolate in MDCK cells A/NIB/23/89M (H1N1) was adapted to mice by serial passaging through mouse lungs. The adaptation enhanced the viral pathogenicity for mice, but preserved the virus receptor binding phenotype, preferential binding to 2-6-linked sialic acid receptors and low affinity for 2-3-linked receptors. Sequencing of the HA gene of the mouse-adapted virus A/NIB/23/89-MA revealed a loss of the glycosylation sites in positions 94 and 163 of HA1 and substitutions 275Asp-->Gly in HA1 and 145Asn-->Asp in HA2. The four mouse strains tested differed significantly in their sensitivity to A/NIB/23/89-MA with the sensitivity increasing in the order of BALB/cJCitMoise, C57BL/6LacSto, CBA/CaLacSto and A/SnJCitMoise strains. Testing of protective efficacy of the polyacrylamide conjugate bearing Neu5Acalpha2-6Galbeta1-4GlcNAc trisaccharide under conditions of lethal or sublethal virus infection demonstrated a strong protective effect of this preparation. In particular, aerosol treatment of mice with the polymeric attachment inhibitor on 24-110 h after infection completely prevented mortality in sensitive animals and lessened disease symptoms in more resistant mouse strains.


Assuntos
Amino Açúcares/uso terapêutico , Vírus da Influenza A Subtipo H1N1/fisiologia , Infecções por Orthomyxoviridae/prevenção & controle , Substâncias Protetoras/uso terapêutico , Receptores Virais/metabolismo , Amino Açúcares/química , Animais , Antivirais/uso terapêutico , Vírus da Influenza A Subtipo H1N1/efeitos dos fármacos , Camundongos , Infecções por Orthomyxoviridae/patologia , Polímeros/administração & dosagem , Polímeros/química , Replicação Viral
10.
Biochemistry (Mosc) ; 70(3): 330-8, 2005 Mar.
Artigo em Inglês | MEDLINE | ID: mdl-15823088

RESUMO

Elimination of apoptotic bodies is one of the important functions of macrophages. The aim of this work was to study the role of macrophage lectins in this process. Macrophage lectins were probed with neoglycoconjugates Glyc-PAA-fluo where carbohydrate is linked to fluorescein-labeled polyacrylamide (MW 30 kD). It was shown that neoglycoconjugates containing a Neu5Acalpha2-3Gal fragment bound to macrophages isolated from blood of healthy donors. Besides, carbohydrate chains containing the same fragment were revealed on apoptotic bodies. Phagocytosis of apoptotic bodies by macrophages was inhibited with sialooligosaccharide ligands of siglec-5 and MAbs to siglec-5. Thus, siglec-5 expressed on macrophages could participate in phagocytosis of apoptotic bodies. In addition, the role of siglecs in engulfment of apoptotic bodies by tumor-associated macrophages was studied. The phagocytic potency of macrophages isolated from blood of breast cancer patients was lower than engulfment ability of macrophages obtained from healthy donors and depended on tumor degree. Staining of macrophages obtained from blood of tumor patients with sialylated Glyc-PAA-fluo probes was more intense than that of macrophages from healthy donors; phagocytosis of apoptotic bodies by tumor-associated macrophages was inhibited by carbohydrates that are known to be ligands for siglecs.


Assuntos
Apoptose , Lectinas/fisiologia , Macrófagos/fisiologia , Glicoproteínas de Membrana/fisiologia , Fagocitose/fisiologia , Receptores Imunológicos/fisiologia , Ácidos Siálicos/fisiologia , Resinas Acrílicas/metabolismo , Neoplasias da Mama , Linhagem Celular Tumoral , Fluoresceína-5-Isotiocianato , Glicoconjugados/metabolismo , Humanos , Lectina 1 Semelhante a Ig de Ligação ao Ácido Siálico
11.
Virology ; 326(2): 310-6, 2004 Sep 01.
Artigo em Inglês | MEDLINE | ID: mdl-15302215

RESUMO

To characterize differences in the receptor-binding specificity of H5N1 chicken viruses and viruses of aquatic birds, we used a panel of synthetic polyacrylamide (PAA)-based sialylglycopolymers that carried identical terminal Neu5Acalpha2-3Gal fragments but varied by the structure of the next saccharide residues. A majority of duck viruses irrespective of their HA subtype, bound with the highest affinity to trisaccharide Neu5Acalpha2-3Galbeta1-3GlcNAc, suggesting that these viruses preferentially recognize sialyloligosaccharide receptors with type 1 core (Galbeta1-3GlcNAc). Substitution of 6-hydroxyl group of GlcNAc residue of tested sialylglycopolymers by 6-sulfo group had little effect on receptor binding by duck viruses. By contrast, H5N1 chicken and human viruses isolated in 1997 in Hong Kong preferred receptors with type 2 core (Galbeta1-4GlcNAcbeta) and bound sulfated trisaccharide Neu5Acalpha2-3Galbeta1-4(6-HSO3)GlcNAcbeta (6-Su-3'SLN) with the extraordinary high affinity. Another chicken virus, A/FPV/Rostok/34 (H7N1), and several mammalian viruses also displayed an increased affinity for sulfated sialyloligosaccharide receptor. The binding of chicken and mammalian viruses to tracheal epithelial cells of green monkey decreased after treatment of cells with glucosamine-6-sulfatase suggesting the presence of 6-O-Su-3'SLN determinants in the airway epithelium. It remains to be seen whether existence of the 6-O-Su-3'SLN groups in the human airway epithelial cells might facilitate infection of humans with H5N1 chicken viruses.


Assuntos
Virus da Influenza A Subtipo H5N1 , Vírus da Influenza A/metabolismo , Lactose/análogos & derivados , Lactose/metabolismo , Receptores Virais/metabolismo , Animais , Sequência de Carboidratos , Membrana Celular/metabolismo , Células Cultivadas , Galinhas/virologia , Chlorocebus aethiops , Patos/virologia , Células Epiteliais/virologia , Gangliosídeos/metabolismo , Influenza Aviária/transmissão , Influenza Aviária/virologia , Lactose/química , Dados de Sequência Molecular , Oligossacarídeos/química , Oligossacarídeos/metabolismo , Receptores Virais/química , Trissacarídeos/metabolismo , Replicação Viral
12.
Bioorg Khim ; 30(2): 174-81, 2004.
Artigo em Russo | MEDLINE | ID: mdl-15143673

RESUMO

A method for the synthesis of photoaffinity neoglycolipid probes with a highly efficient carbene-generating diazocyclopentadien-2-ylcarbonyl (Dcp) label, which can be radioiodinated under standard oxidation conditions, was developed. The probes are intended for incorporation into the lipid bilayer. They are lipophilic glycoconjugates on the basis of an amphiphilic aglycone built up from a diacylglycerol and a polyethylene glycol spacer (with a polymerization degree of 9-16) bearing the Dcp label at the terminal unit. The location of the label in the aglycone provides the possibility of one-step preparation of a wide range of probes using various carbohydrate synthons. We have synthesized photoaffinity neoglycoconjugates containing the oligosaccharides: sialyl LewisX tetrasaccharide and A trisaccharide, which is specific to some tumor cells. A probe containing an inactive pentaol (aminodeoxyglucitol) was also synthesized to detect nonspecific binding. The Dcp label is bound to the probe molecule by ester bond; its lability under alkaline conditions facilitates the analysis of cross-linked products after photoaffinity labeling. The English version of the paper: Russian Journal of Bioorganic Chemistry, 2004, vol. 30, no. 2; see also http://www.maik.ru.


Assuntos
Glicolipídeos/síntese química , Lectinas/química , Proteínas de Membrana/química , Sondas Moleculares , Marcadores de Afinidade , Ressonância Magnética Nuclear Biomolecular , Fotoquímica
13.
Glycoconj J ; 20(2): 83-9, 2004.
Artigo em Inglês | MEDLINE | ID: mdl-15001840

RESUMO

The TF, Tn, and SiaTn glycotopes are frequently expressed in cancer-associated mucins. Antibodies to these glycotopes were found in human serum. A set of polyacrylamide (PAA)--based glycoconjugates was applied to the direct and competitive enzyme-linked immunosorbent assays (ELISA) to characterize the specificity of serum IgG antibodies. The anti-TF, -Tn and -SiaTn IgG were affinity purified from serum of cancer patients and characterized using PAA-conjugates and free saccharides. The anti-TF and -Tn antibodies were shown to be specific. The anti-TF IgG bound both Galbeta1-3GalNAcalpha- and Galbeta1-3GalNAcbeta-PAA, the latter was three-four times more effective inhibitor of antibody binding. The anti-Tn IgG reacted only with GalNAcalpha-PAA. The anti-SiaTn IgG cross-reacted with Tn-PAA but SiaTn-PAA was five-six times more effective inhibitor in a competitive assay. The IC50 values for PAA-conjugates with the corresponding antibodies typically ranged from 2 to 5 x 10(-8) M. The antibodies display a low specificity to mucin-type glycoconjugates in comparison with PAA-conjugates as was shown for mucins isolated from human malignant tumor tissues, ovine submaxillary mucin (OSM) and asialo-OSM. The unusual IgG-antibody specificity to GalNAcbeta and GalNAcbeta1-3GalNAcbeta ligands was found in human serum.


Assuntos
Especificidade de Anticorpos/imunologia , Carboidratos/imunologia , Glicoconjugados/imunologia , Imunoglobulina G/imunologia , Resinas Acrílicas/química , Epitopos/imunologia , Glicoconjugados/química , Humanos , Imunoglobulina G/sangue , Sondas Moleculares , Mucinas/imunologia , Soro/imunologia
14.
Lab Chip ; 3(4): 260-5, 2003 Nov.
Artigo em Inglês | MEDLINE | ID: mdl-15007456

RESUMO

Biotinylated glycoconjugates which were designed as oligosaccharides attached to 30 kDa polyacrylamide were coated on a microarray platform XNAonGOLD, which was developed earlier for an oligonucleotide assay. The specificity of antibodies to carbohydrate antigens was analyzed using the glyco-microarray. Comparison of the obtained results with those of common 96-well plate ELISA completely coincided with the found antibody specificities. However, parameters such as the analytical sensitivity of the method and the amount of biotinylated material coated on the microarray platform proved to be worse than expected.


Assuntos
Proteínas de Transporte/análise , Microcomputadores , Análise Serial de Proteínas , Receptores de Superfície Celular , Anticorpos/análise , Especificidade de Anticorpos , Antígenos/química , Biotina/química , Carboidratos/imunologia , Ensaio de Imunoadsorção Enzimática , Indicadores e Reagentes , Oligossacarídeos/química , Espectrometria de Fluorescência
15.
Bioorg Khim ; 28(6): 518-34, 2002.
Artigo em Russo | MEDLINE | ID: mdl-12528464

RESUMO

Neoglycoconjugates containing 4, 8, 16, 32, and 64 terminal residues of B-disaccharide (BDI) or N-acetylneuraminic acid (Neu5Ac) attached to poly(aminoamide)-type dendrimers (PAMAMs) were synthesized. The ability of BDI conjugates to bind natural xenoantibodies (anti-BDI antibodies) and the ability of Neu5Ac conjugates to inhibit the hemagglutinin-mediated adhesion of influenza virus were studied. The biological activity of PAMAM conjugates turned out to be higher than that of free carbohydrate ligands, but less than that of multivalent glycoconjugates based on other types of synthetic polymeric carriers. A conformational analysis of PAMAM matrices and resulting conjugates was performed to determine the statistical distances between carbohydrate ligands. The computations revealed the tendency of the PAMAM chains toward compaction and formation of dense globules. The process results in a decrease in the distances between the carbohydrate ligands in the conjugates and, hence, could affect the ability of glycoconjugates to efficiently bind the polyvalent carbohydrate-recognizing proteins. The English version of the paper: Russian Journal of Bioorganic Chemistry, 2002, vol. 28, no. 6; see also http://www.maik.ru.


Assuntos
Antivirais/síntese química , Glicoconjugados/síntese química , Imunossupressores/síntese química , Poliaminas/química , Anticorpos Heterófilos/sangue , Anticorpos Heterófilos/imunologia , Antivirais/química , Antivirais/farmacologia , Dendrímeros , Dissacaridases/química , Glicoconjugados/química , Glicoconjugados/farmacologia , Humanos , Imunossupressores/química , Imunossupressores/farmacologia , Ligantes , Conformação Molecular , Estrutura Molecular , Ácido N-Acetilneuramínico/química , Orthomyxoviridae/efeitos dos fármacos
16.
Bioorg Khim ; 23(1): 61-74, 1997 Jan.
Artigo em Russo | MEDLINE | ID: mdl-9139645

RESUMO

Spacered terminal disaccharide of Forssman's antigen GalNAc alpha 1-3GalNAc beta 1-Osp, its analog GalNAc alpha 1-3GalNAc alpha 1-Osp, and disaccharides Gal beta 1-3GalNAc beta 1-Osp and Gal alpha 1-3GalNAc alpha 1-Osp [where sp denotes the (CH2)3NHCOCF3 spacer] were synthesized. Spacered disaccharides were obtained from the (3-trifluoroacetamidopropyl)-2-acetamido-4,6-O-benzylidene-2-deoxy-beta-D- galactopyranoside and its alpha- and beta-analogs in which the 2-azido group was substituted for the 2-acetamido group. The azide glycosyl acceptors gave higher yields of the disaccharides. Azide glycosyl acceptors were prepared by the stereoselective glycosylation of 3-trifluoroacetamidopropanol with a mixture of 1-O-acetates of the 2-azido-3,4,6-tri-O-acetyl-2-deoxy-D-galactopyranose anomers in the presence of Lewis acids. Disaccharides Gal alpha 1-3GalNAc and GalNAc alpha 1-3GalNAc were obtained from the benzyl 2-acetamido-4,6-O-benzylidene-2-deoxy-alpha-D-galactopyranoside.


Assuntos
Dissacarídeos/síntese química , Antígeno de Forssman/química , Glicosídeos/química , Sequência de Carboidratos , Dissacarídeos/química , Dados de Sequência Molecular
SELEÇÃO DE REFERÊNCIAS
DETALHE DA PESQUISA