Search results for "Structure-Activity relationship"

showing 10 items of 743 documents

Structure-function analysis of peroxisomal ATP-binding cassette transporters using chimeric dimers

2014

Background: Peroxisomal ABC transporters are predicted to function as homodimers in mammals. [br/] Results: ABCD1 interacts with ABCD2. Chimeric proteins mimicking full-length dimers represent novel tools for functional study. Artificial homodimers and heterodimers are functional. [br/] Conclusion: Interchangeability between ABCD1 and ABCD2 is confirmed, but PUFA transport depends on ABCD2. [br/] Significance: For the first time, heterodimers in mammals are proven to be functional.[br/] ABCD1 and ABCD2 are two closely related ATP-binding cassette half-transporters predicted to homodimerize and form peroxisomal importers for fatty acyl-CoAs. Available evidence has shown that ABCD1 and ABCD2 …

[SDV.BA] Life Sciences [q-bio]/Animal biologyprotéine chimereanimal diseasesATP-binding cassette transporterProximity ligation assayProtein Chimerabiochimie structurale[ SDV.BA ] Life Sciences [q-bio]/Animal biologyPolymerase Chain ReactionBiochemistryGreen fluorescent proteininteraction moléculaireMice[ CHIM.OTHE ] Chemical Sciences/Otherhomodimèrereproductive and urinary physiologyAnimal biologyhétérodimèrechemistry.chemical_classification[SDV.BA]Life Sciences [q-bio]/Animal biologymammifèreTransfectionPeroxisomeprotéine de fusionBiochemistry[CHIM.OTHE] Chemical Sciences/OtherDimerizationPlasmidsABC Transporter;Fatty Acid;Peroxisome;Protein Chimera;Protein-Protein Interactiontransporteur abcBiologyPeroxisomeCell LineProtein–protein interactionStructure-Activity RelationshipMembrane BiologyBiologie animaleparasitic diseasesAutre (Chimie)PeroxisomesAnimalsHumansMolecular BiologyDNA PrimersBase SequenceABCD2fungiABCD1Fatty acidCell BiologyFusion proteinRatsProtein-Protein InteractionABC TransporterchemistryATP-Binding Cassette TransportersOther[CHIM.OTHE]Chemical Sciences/OtherFatty Acid
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Rbt1 Protein Domains Analysis in Candida albicans Brings Insights into Hyphal Surface Modifications and Rbt1 Potential Role during Adhesion and Biofi…

2013

Cell wall proteins are central to the virulence of Candida albicans. Hwp1, Hwp2 and Rbt1 form a family of hypha-associated cell surface proteins. Hwp1 and Hwp2 have been involved in adhesion and other virulence traits but Rbt1 is still poorly characterized. To assess the role of Rbt1 in the interaction of C. albicans with biotic and abiotic surfaces independently of its morphological state, heterologous expression and promoter swap strategies were applied. The N-terminal domain with features typical of the Flo11 superfamily was found to be essential for adhesiveness to polystyrene through an increase in cell surface hydrophobicity. A 42 amino acid-long domain localized in the central part o…

[SDV]Life Sciences [q-bio]lcsh:MedicinebiofilmCell membraneadhésionCandida albicanslcsh:ScienceCandida albicansRecombination Genetic0303 health sciencesFungal proteinMultidisciplinaryCandida albicans;cell wall;protein;Rbt1;adhesion;biofilmbiologyFlow Cytometry3. Good healthCell biologyTransport proteinProtein Transportadhesionmedicine.anatomical_structureprotéineparoi cellulaireHydrophobic and Hydrophilic InteractionsResearch ArticleProtein domainSaccharomyces cerevisiaeHyphaeSaccharomyces cerevisiaeFungal ProteinsStructure-Activity Relationship03 medical and health sciencesCell AdhesionmedicineHumansAmino Acid SequenceCell adhesion030304 developmental biologySequence Homology Amino Acid030306 microbiologyCell Membranelcsh:Rfungibiology.organism_classificationRbt1Protein Structure TertiaryMembrane proteinBiofilmsPolystyrenescell walllcsh:Qprotein
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α-Aminoalkylphosphonates as a tool in experimental optimisation of P1 side chain shape of potential inhibitors in S1 pocket of leucine- and neutral a…

2005

Abstract The synthesis and biological activity studies of the series of structurally different α-aminoalkylphosphonates were performed in order to optimise the shape of the side chain of the potential inhibitors in S1 pocket of leucine aminopeptidase [E.C.3.4.11.1]. Analysis of a series of compounds with aromatic, aliphatic and alicyclic P1 side chains enabled to find out the structural features, optimal for that fragment of inhibitors of LAP. The most active among all investigated compounds were the phosphonic analogues of homo-tyrosine ( K i  = 120 nM) and homo-phenylalanine ( K i  = 140 nM), which even as racemic mixtures were better inhibitors in comparison with the best till now-phosph…

aminophosphonatesStereochemistryleucine aminopeptidaseOrganophosphonatesKidneyAminopeptidasesChemical synthesisAminopeptidaseLeucyl AminopeptidaseStructure-Activity RelationshipAlicyclic compoundLeucineDrug DiscoverySide chainAnimalsLeucyl aminopeptidasePharmacologychemistry.chemical_classificationBinding SitesMolecular StructureAminopeptidase NOrganic ChemistryBiological activityGeneral MedicineHydrogen-Ion Concentrationaminopeptidase NinhibitorEnzymechemistryLeucineEuropean Journal of Medicinal Chemistry
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Regulation of the alpha-secretase ADAM10 by its prodomain and proprotein convertases.

2001

SPECIFIC AIMSTo identify the proprotein convertases responsible for maturation of the α-secretase ADAM10, we investigated the influence of PC7 and furin on ADAM10 processing and the resulting effect on amyloid precursor protein cleavage. We also examined the functional role of the ADAM10 prodomain by coexpression of a prodomain-deleted ADAM10 mutant together with its prodomain in trans.PRINCIPAL FINDINGS1. ADAM10 is proteolytically processed by PC7 and furinThe disintegrin metalloproteinase ADAM10 possesses α-secretase activity as well as a potential proprotein convertase recognition sequence (RKKR) after its prodomain. By amino-terminal sequencing of ADAM10 purified from bovine kidney plas…

animal structuresADAM10Blotting WesternKidneyTransfectionBiochemistryCell LineAmyloid beta-Protein PrecursorStructure-Activity RelationshipZymogenEndopeptidasesGeneticsAmyloid precursor proteinAnimalsAspartic Acid EndopeptidasesHumansSubtilisinsProtein PrecursorsMolecular BiologyFurinFurinbiologyChemistryProprotein convertaseEmbryo MammalianRecombinant ProteinsEnzyme ActivationBiochemistryAlpha secretaseMutagenesisbiology.proteinCattleAmyloid Precursor Protein SecretasesProprotein ConvertasesAmyloid precursor protein secretaseBiotechnologyFASEB journal : official publication of the Federation of American Societies for Experimental Biology
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Hsp60, a Novel Target for Antitumor Therapy: Structure-Function Features and Prospective Drugs Design

2013

Heat shock protein 60 kDa (Hsp60) is a chaperone classically believed to be involved in assisting the correct folding of other mitochondrial proteins. Hsp60 also plays a role in cytoprotection against cell stressors, displaying for example, antiapoptotic potential. Despite the plethora of studies devoted to the mechanism of Hsp60's function, especially in prokaryotes, fundamental issues still remain unexplored, including the definition of its role in cancer. Key questions still unanswered pertain to the differences in structure-function features that might exist between the well-studied prokaryotic GroEL and the largely unexplored eukaryotic Hsp60 proteins. In this article we discuss these …

animal structuresBinding pocketCellAntineoplastic Agentschemical and pharmacologic phenomenaComputational biologyBiologyBioinformaticsFunctional domaincomplex mixturesChaperoninStructure-Activity RelationshipNeoplasmsHeat shock proteinDrug DiscoverymedicineHumansPharmacologyCompound dockingSettore BIO/16 - Anatomia UmanaCell growthfungiSettore CHIM/06 - Chimica OrganicaChaperonin 60Hsp60Settore CHIM/08 - Chimica FarmaceuticaCytoprotectionGroELmedicine.anatomical_structureSettore CHIM/03 - Chimica Generale E InorganicaCancer treatmentDrug DesignChaperone (protein)biology.proteinHSP60Protein foldingEpolactaeneCurrent Pharmaceutical Design
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New 1,2,4-oxadiazole nortopsentin derivatives with cytotoxic activity

2019

New analogs of nortopsentin, a natural 2,4-bis(3&prime

anti-cancer agentCell SurvivalAnti-cancer agentsPharmaceutical ScienceAntineoplastic AgentsAntiproliferative activity01 natural sciencesArticlechemistry.chemical_compoundStructure-Activity RelationshipMarine alkaloidsSettore BIO/10 - BiochimicaDrug DiscoveryMoietyHumansPharmacology Toxicology and Pharmaceutics (miscellaneous)lcsh:QH301-705.5Cell ProliferationIndole testMolecular Structure010405 organic chemistryAcridine orangeImidazoles2 4-oxadiazole derivativesnortopsentin analogs2 4-oxadiazole derivatives; Anti-cancer agents; Antiproliferative activity; Marine alkaloids; Nortopsentin analogs 1; Antineoplastic Agents; Caco-2 Cells; Cell Cycle Checkpoints; Cell Proliferation; Cell Survival; HCT116 Cells; Humans; Imidazoles; MCF-7 Cells; Molecular Structure; Structure-Activity RelationshipPhosphatidylserineCell Cycle CheckpointsNortopsentin analogs 1HCT116 CellsSettore CHIM/08 - Chimica Farmaceutica0104 chemical sciences124-oxadiazole derivative010404 medicinal & biomolecular chemistrychemistryBiochemistry124-oxadiazole derivativeslcsh:Biology (General)ApoptosisCell cultureCancer cellMCF-7 CellsMarine alkaloid2 4-oxadiazole derivativeCaco-2 CellsEthidium bromide
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Dipeptides of S-Substituted Dehydrocysteine as Artzyme Building Blocks: Synthesis, Complexing Abilities and Antiproliferative Properties †

2021

Background: Dehydropeptides are analogs of peptides containing at least one conjugate double bond between α,β-carbon atoms. Its presence provides unique structural properties and reaction centre for chemical modification. In this study, the series of new class of dipeptides containing S-substituted dehydrocysteine with variety of heterocyclic moieties was prepared. The compounds were designed as the building blocks for the construction of artificial metalloenzymes (artzymes). Therefore, the complexing properties of representative compounds were also evaluated. Furthermore, the acknowledged biological activity of natural dehydropeptides was the reason to extend the study for antiproliferativ…

antiproliferative activityBALB 3T3 CellsDouble bondPotentiometric titrationSulforhodamine BTriazoleAntineoplastic Agents010402 general chemistry01 natural sciencesCatalysisArticlelcsh:ChemistryInorganic ChemistryMiceStructure-Activity Relationshipchemistry.chemical_compoundElimination reactionCell Line TumorAnimalsHumansChelationCysteinePhysical and Theoretical Chemistrydehydrocysteinelcsh:QH301-705.5Molecular BiologySpectroscopyCell Proliferationchemistry.chemical_classification010405 organic chemistryOrganic ChemistryChemical modificationDipeptidesGeneral MedicineHydrogen-Ion ConcentrationCombinatorial chemistryEnzymes0104 chemical sciencesComputer Science Applicationsdehydropeptideslcsh:Biology (General)lcsh:QD1-999chemistrycomplexing agentaddition-elimination reactionDrug Screening Assays AntitumorCopperConjugateInternational Journal of Molecular Sciences
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Synthesis and antiproliferative activity of the ring system [1,2]oxazolo[4,5-g]indole.

2012

Brand new ring: A series of 27 derivatives of the new ring system [1,2]oxazolo[4,5-g]indole were conveniently prepared and tested at the NCI for antiproliferative studies. Several of them showed good inhibitory activity toward all tested cell lines, reaching GI50 values generally at the micromolar and sub-micromolar levels and in some cases at nanomolar concentrations. The mean GI50 values, calculated on the full panel, were in the range 0.25-7.08 μM.

antiproliferative activityIndolesStereochemistryhydroxylamine hydrochloridesAntineoplastic AgentsRing (chemistry)Biochemistrychemistry.chemical_compoundStructure-Activity RelationshipCell Line TumorNeoplasms2]oxazolo[4Drug Discoveryantiproliferative activity; combretastatin A-4; enaminoketones; hydroxylamine hydrochlorides; [1; 2]oxazolo[4; 5-g]indolesStructure–activity relationshipHumanscombretastatin A-4General Pharmacology Toxicology and PharmaceuticsOxazolesCell ProliferationPharmacologyCombretastatin A-4Indole testantiproliferative activity combretastatin A-4 enaminoketones hydroxylamine hydrochlorides[12]oxazolo[45-g]indolesOrganic ChemistrySettore CHIM/08 - Chimica Farmaceuticachemistry5-g]indolesenaminoketonesMolecular Medicine[1Drug Screening Assays AntitumorChemMedChem
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1-methil-3H-pyrazolo[1-2-a]benzo[1-2-3-4]tetrazin-3-ones, design synthesis and biological activity of new antitumoral agents

2005

1-Methylpyrazolo[1,2-a]benzo[1,2,3,4]tetrazin-3-ones 4, synthesized in good to excellent yields, were designed as novel alkylating agents because of their peculiar chemical behavior. All derivatives showed antiproliferative activity against more than 50 types of tumor cell lines with GI50 reaching sub-micromolar values. SAR studies revealed that the presence of a chlorine atom is well-tolerated in both positions 8 and 9, whereas in the case of the methyl group, switching from the 8 to the 9 position gives rise to the most active compound of the series, 4g, either for the number of cell lines inhibited and for selectivity against leukaemia and renal cancer subpanels. COMPARE and 3D-MIND comp…

antiproliferative activityQuantitative structure–activity relationshipStereochemistry2-a]benzotetrazinoneQuantitative Structure-Activity RelationshipRifamycinsAntineoplastic Agents1-Methylpyrazolo[12-a]benzo[1234]tetrazin-3-oneChemical synthesischemistry.chemical_compoundantiproliferativeCell Line TumorDrug DiscoveryCOMPARE and 3D-MIND analysisHumansComputer Simulationpyrazolo[1CytotoxicityBiological activityCytidinechemistryDrug Designantitumor agentMolecular MedicinePyrazolesDrug Screening Assays AntitumorSelectivityHeterocyclic Compounds 3-RingMethyl group
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3-(6-Phenylimidazo [2,1-

2019

A new series of imidazo[2,1-b][1,3,4]thiadiazole derivatives was efficiently synthesized and screened for their in vitro antiproliferative activity on a panel of pancreatic ductal adenocarcinoma (PDAC) cells, including SUIT-2, Capan-1 and Panc-1. Compounds 9c and 9l, showed relevant in vitro antiproliferative activity on all three pre-clinical models with half maximal inhibitory concentration (IC50) ranging from 5.11 to 10.8 µM, while the compounds 9e and 9n were active in at least one cell line. In addition, compound 9c significantly inhibited the migration rate of SUIT-2 and Capan-1 cells in the scratch wound-healing assay. In conclusion, our results will support further studies to increa…

antiproliferative activitymigration assayIndolesimidazo[21-b][134]thiadiazole derivativespancreatic cancerAntineoplastic AgentsAdenocarcinomaindole compoundsArticlePancreatic NeoplasmsresistanceStructure-Activity RelationshipTumor Cells CulturedHumansDrug Screening Assays AntitumorCarcinoma Pancreatic DuctalCell ProliferationMolecules (Basel, Switzerland)
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