Search results for "Low affinity"

showing 5 items of 5 documents

Validation strategies for antibodies targeting modified ribonucleotides

2020

Chemical modifications are found on almost all RNAs and affect their coding and noncoding functions. The identification of m6A on mRNA and its important role in gene regulation stimulated the field to investigate whether additional modifications are present on mRNAs. Indeed, modifications including m1A, m5C, m7G, 2′-OMe, and Ψ were detected. However, since their abundances are low and tools used for their corroboration are often not well characterized, their physiological relevance remains largely elusive. Antibodies targeting modified nucleotides are often used but have limitations such as low affinity or specificity. Moreover, they are not always well characterized and due to the low abun…

chemistry.chemical_classificationRegulation of gene expression0303 health sciencesMessenger RNAbiologyNucleotidesmedicine.drug_class030302 biochemistry & molecular biologyMethodComputational biologyRibonucleotidesMonoclonal antibodyAntibodies03 medical and health sciencesLow affinitychemistrybiology.proteinmedicineRNANucleotideRNA MessengerAntibodyMolecular Biology030304 developmental biologyRNA
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Interaction between odorants and proteins involved in the perception of smell: the case of odorant-binding proteins probed by molecular modelling and…

2012

A joint approach that combines molecular modelling and fluorescence spectroscopy is used to study the affinity of an odorant binding protein towards various odorant molecules. We focus on the capability of molecular modelling to rank odorants according to their affinity with this protein, which is involved in the sense of smell. Although ligand-based approaches are unable to propose an accurate model attending to the strength of the bond with the odorant-binding protein, receptor-based structures considering either static or dynamic structure of the protein perform equally to discriminate between good, medium and low affinity odorants. Such approaches will be useful for further rational des…

0303 health sciencesbiology010405 organic chemistryOdorant bindingChemistrymusculoskeletal neural and ocular physiologyRational designGeneral ChemistryComputational biologyOlfactionLigand (biochemistry)01 natural sciences0104 chemical sciences03 medical and health sciencesLow affinityBiochemistryOdorant-binding proteinbiology.proteinpsychological phenomena and processes030304 developmental biologyFood ScienceFlavour and Fragrance Journal
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The binding of intravenous and oral biliary contrast agents to human and bovine serum albumin

1978

The binding of two homologous series of oral and intravenous biliary contrast agents to human and bovine serum albumin was investigated using the gel filtration technique. All intravenous compounds are bound to human serum albumin via one high affinity and several low affinity binding sites. Within the concentration range investigated, about 3--5 high affinity binding sites for the oral compounds were found on human serum albumin. In general, the intravenous compounds have a greater affinity for human serum albumin than the oral compounds. No significant differences were found for the binding of the oral compounds to human or bovine serum albumin, while the intravenous compounds have a high…

High affinity bindingSize-exclusion chromatographySerum albuminAdministration OralContrast MediaPlasma protein bindingIn Vitro TechniquesPharmacologyLow affinitymedicineAnimalsHumansBovine serum albuminBinding siteBiliary TractSerum AlbuminPharmacologyBinding SitesbiologyChemistrySerum Albumin BovineGeneral MedicineHydrogen-Ion ConcentrationHuman serum albuminRadiographySolubilityBiochemistryInjections Intravenousbiology.proteinCattleProtein Bindingmedicine.drugNaunyn-Schmiedeberg's Archives of Pharmacology
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Pheromone-binding proteins of scarab beetles.

1998

: We have characterized Pheromone binding proteins (PBPs) present in the antennae of several species of scarab beetles. In most cases there was only one class of PBP, which was expressed in both sexes. Both Anomala osakana and Popillia japonica possess a single PBP, highly homologous to each other. In each species the same PBP seems to recognize both enantiomers of japonilure, which have opposite biological functions, i.e., the sex Pheromone and the behavioral antagonist (stop signal). The purified PBP of A. osakana binds both enantiomers apparently with the same low affinity. Unexpectedly, these ligands were bound by moth PBPs, which utilize Pheromones with unrelated structures. These find…

biologyAnomala osakanaLigandGeneral Neurosciencebiochemical phenomena metabolism and nutritionbiology.organism_classificationGeneral Biochemistry Genetics and Molecular BiologyChemoreceptor CellsPheromonesColeopteraLow affinityHistory and Philosophy of ScienceBiochemistrySex pheromoneBotanyPopilliapolycyclic compoundsHomologous chromosomebacteriaAnimalsInsect ProteinsPheromone bindingEnantiomerAnnals of the New York Academy of Sciences
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2,3-Dihydrobenzofuran privileged structures as new bioinspired lead compounds for the design of mPGES-1 inhibitors

2016

International audience; 2,3-Dihydrobenzofurans are proposed as privileged structures and used as chemical platform to design small compound libraries. By combining molecular docking calculations and experimental verification of biochemical interference, we selected some potential inhibitors of microsomal prostaglandin E2 synthase (mPGES)-1. Starting from low affinity natural product 1, by our combined approach we identified the compounds 19 and 20 with biological activity in the low micromolar range. Our data suggest that the 2,3-dihydrobenzofuran derivatives might be suitable bioinspired lead compounds for development of new generation mPGES-1 inhibitors with increased affinity.

0301 basic medicine300323-Dihydrobenzofuran privileged structure; Cancer; Inflammation; Molecular docking; mPGES-1 inhibitors; Biochemistry; Clinical Biochemistry; Molecular Biology; Molecular Medicine; Organic Chemistry; Drug Discovery3003 Pharmaceutical Science; 3003Amino Acid MotifsClinical BiochemistryGene ExpressionPharmaceutical Science01 natural sciencesClinical biochemistryBiochemistry[ CHIM ] Chemical SciencesProtein Structure Secondary[ SDV.CAN ] Life Sciences [q-bio]/Cancerchemistry.chemical_compoundLow affinityDrug DiscoveryEnzyme Inhibitors23-Dihydrobenzofuran privileged structure; Molecular docking; mPGES-1 inhibitors; Cancer; InflammationProstaglandin-E SynthasesCancerAnti-Inflammatory Agents Non-SteroidalBiological activityProto-Oncogene Proteins c-metIntramolecular OxidoreductasesMolecular Docking SimulationMolecular dockingMolecular Medicinelipids (amino acids peptides and proteins)Cell SurvivalStereochemistryMolecular Sequence Data2Antineoplastic Agents[SDV.CAN]Life Sciences [q-bio]/Cancer3-Dihydrobenzofuran privileged structureInhibitory Concentration 50Structure-Activity Relationship03 medical and health sciencesCell Line TumorMicrosomesHumans[CHIM]Chemical SciencesMolecular BiologyBenzofuransInflammationNatural product010405 organic chemistryDrug Discovery3003 Pharmaceutical ScienceOrganic ChemistryEpithelial CellsmPGES-1 inhibitorsCombinatorial chemistryCombined approach0104 chemical sciences030104 developmental biologychemistryDrug DesignDrug Screening Assays Antitumor
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