Search results for "AMINO ACID"

showing 10 items of 3965 documents

Searching for Chymase Inhibitors among Chamomile Compounds Using a Computational-Based Approach

2018

Inhibitors of chymase have good potential to provide a novel therapeutic approach for the treatment of cardiovascular diseases. We used a computational approach based on pharmacophore modeling, docking, and molecular dynamics simulations to evaluate the potential ability of 13 natural compounds from chamomile extracts to bind chymase enzyme. The results indicated that some chamomile compounds can bind to the active site of human chymase. In particular, chlorogenic acid had a predicted binding energy comparable or even better than that of some known chymase inhibitors, interacted stably with key amino acids in the chymase active site, and appeared to be more selective for chymase than other …

0301 basic medicineProteaseschlorogenic acidlcsh:QR1-502030204 cardiovascular system & hematologyMolecular Dynamics SimulationCrystallography X-RayLigandsBiochemistrylcsh:MicrobiologyArticleSerine03 medical and health sciences0302 clinical medicineChymasesCatalytic DomainHumanschamomilecardiovascular diseases; chamomile; chlorogenic acid; chymase; docking; matricin; molecular dynamics simulations; pharmacophore; Biochemistry; Molecular BiologyEnzyme InhibitorsMolecular Biologychymasechemistry.chemical_classificationBinding SitesbiologypharmacophoreChymaseActive sitemolecular dynamics simulationsmatricinAmino acidcardiovascular diseasesMolecular Docking Simulation030104 developmental biologyEnzymechemistryBiochemistryDocking (molecular)dockingbiology.proteinPharmacophoreBiomolecules
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Host Cell Calpains Can Cleave Structural Proteins from the Enterovirus Polyprotein

2019

Enteroviruses are small RNA viruses that cause diseases with various symptoms ranging from mild to severe. Enterovirus proteins are translated as a single polyprotein, which is cleaved by viral proteases to release capsid and nonstructural proteins. Here, we show that also cellular calpains have a potential role in the processing of the enteroviral polyprotein. Using purified calpains 1 and 2 in an in vitro assay, we show that addition of calpains leads to an increase in the release of VP1 and VP3 capsid proteins from P1 of enterovirus B species, detected by western blotting. This was prevented with a calpain inhibitor and was dependent on optimal calcium concentration, especially for calpa…

0301 basic medicineProteasesentsyymitRNA virusviruksetvirusesPeptideCleavage (embryo)infektiotMass SpectrometryArticle03 medical and health sciencesViral ProteinsCapsidVirologyCleaveEnterovirus InfectionsAnimalsHumansCells CulturedGlycoproteinsPolyproteinschemistry.chemical_classification030102 biochemistry & molecular biologybiologyChemistryCalpainenterovirusvirus diseasesRNA virusCalpainbiochemical phenomena metabolism and nutritionbiology.organism_classificationAmino acidRatspolyproteinenterovirukset030104 developmental biologyInfectious DiseasesBiochemistryCapsidproteolytic processingProteolysisbiology.proteinCapsid ProteinsproteiinitPeptidescalpain
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Lunasin is a redox sensitive intrinsically disordered peptide with two transiently populated α-helical regions.

2016

Lunasin is a 43 amino acid peptide with anti-cancer, antioxidant, anti-inflammatory and cholesterol-lowering properties. Although the mechanism of action of lunasin has been characterized to some extent, its exact three-dimensional structure as well as the function of the N-terminal sequence remains unknown. We established a novel method for the production of recombinant lunasin that allows efficient isotope labeling for NMR studies. Initial studies showed that lunasin can exist in a reduced or oxidized state with an intramolecular disulfide bond depending on solution conditions. The structure of both forms of the peptide at pH 3.5 and 6.5 was characterized by CD spectroscopy and multidimen…

0301 basic medicineProtein Conformation alpha-HelicalCircular dichroismPhysiologyBeta sheetPeptideIntrinsically disordered proteinsBiochemistryLunasinAntioxidantsHistones03 medical and health sciencesCellular and Molecular Neuroscience0302 clinical medicineEndocrinologyNeoplasmsAnticarcinogenic AgentsHumansAmino Acid SequenceDisulfidesProtein secondary structureNuclear Magnetic Resonance BiomolecularPlant Proteinschemistry.chemical_classificationChemistryAcetylationNuclear magnetic resonance spectroscopyIntrinsically Disordered Proteins030104 developmental biologyBiochemistry030220 oncology & carcinogenesisBiophysicsSoybean ProteinsPeptidesOxidation-ReductionFunction (biology)Peptides
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In vivo selection of heterotypically interacting transmembrane helices: Complementary helix surfaces, rather than conserved interaction motifs, drive…

2017

Single pass transmembrane proteins make up almost half of the whole transmembrane proteome. Contacts between such bitopic transmembrane proteins are common, and oligomerization of their single transmembrane helix is involved in triggering and regulation of signal transduction across cell membranes. In several recent analyses the distribution of amino acids at helix-helix contact sides has been analyzed, and e.g. a preference of amino acids with small side chains has been identified. Here we select amino acids, amino acid pairings and amino acid motifs, which mediate strong interactions of single-span transmembrane α-helices. Our analysis illustrates an architecture of TM helix dimers that i…

0301 basic medicineProtein Conformation alpha-HelicalDimerAmino Acid MotifsBiophysicsBiologyBiochemistryBordetella pertussisProtein Structure Secondary03 medical and health scienceschemistry.chemical_compoundAmino Acid SequenceAmino Acidschemistry.chemical_classificationCell MembraneMembrane ProteinsCell BiologyTransmembrane proteinAmino acidCrystallographyTransmembrane domain030104 developmental biologyMembrane proteinchemistryProteomeHelixBiophysicsProtein foldingDimerizationBiochimica et biophysica acta. Biomembranes
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The Crystal Structure of Gurmarin, a Sweet Taste–Suppressing Protein: Identification of the Amino Acid Residues Essential for Inhibition

2018

International audience; Gurmarin is a highly specific sweet-taste suppressing protein in rodents that is isolated from the Indian plant Gymnemasylvestre. Gurmarin consists of 35 amino acid residues containing three intramolecular disulfide bridges that form a cystine knot. Here, we report the crystal structure of gurmarin at a 1.45 Å resolution and compare it with previously reported NMR solution structures. The atomic structure at this resolution allowed us to identify a very flexible region consisting of hydrophobic residues. Some of these amino acid residues had been identified as a putative binding site for the rat sweet taste receptor in a previous study. By combining alanine-scanning …

0301 basic medicineProtein ConformationPhysiologyCrystal structureCrystallography X-Ray03 medical and health sciencesBehavioral NeuroscienceGPCRsweet tastetaste receptorPhysiology (medical)goût sucréAnimalsHumansG protein-coupled receptorAmino AcidsBinding siteReceptorNuclear Magnetic Resonance BiomolecularPlant ProteinsGurmarininhibiteur030102 biochemistry & molecular biologybiologyChemistryMutagenesisCystine knotGymnema sylvestreSweet tastebiology.organism_classificationRecombinant ProteinsSensory SystemsRats3. Good healthinhibitorHEK293 Cells030104 developmental biologyBiochemistryGymnema sylvestreknottin[SDV.AEN]Life Sciences [q-bio]/Food and NutritionHydrophobic and Hydrophilic InteractionsChemical Senses
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Quantitative analysis of the impact of a human pathogenic mutation on the CCT5 chaperonin subunit using a proxy archaeal ortholog

2017

The human chaperonin complex is a ~ 1 MDa nanomachine composed of two octameric rings formed from eight similar but non-identical subunits called CCT. Here, we are elucidating the mechanism of a heritable CCT5 subunit mutation that causes profound neuropathy in humans. In previous work, we introduced an equivalent mutation in an archaeal chaperonin that assembles into two octameric rings like in humans but in which all subunits are identical. We reported that the hexadecamer formed by the mutant subunit is unstable with impaired chaperoning functions. This study quantifies the loss of structural stability in the hexadecamer due to the pathogenic mutation, using differential scanning calorim…

0301 basic medicineProtein subunitMutantBiophysicsHeterologousBiochemistryChaperoninChaperoninlcsh:Biochemistry03 medical and health sciencesDSC differential scanning calorimetryCCT% chaperoninPf Pyrococcus furiosusDenaturation (biochemistry)lcsh:QD415-436Molecular Biologylcsh:QH301-705.5DLS dynamic light scatteringbiologyITC isothermal titration calorimetryWild typeIsothermal titration calorimetryCell BiologyChaperonopathiesbiology.organism_classificationProtein calorimetryNeuropathyPyrococcus furiosus030104 developmental biologyBiochemistryBiophysiclcsh:Biology (General)Pyrococcus furiosusChaperonopathieCCT5; Chaperonin; Chaperonopathies; Neuropathy; Protein calorimetry; Pyrococcus furiosus; Biophysics; Biochemistry; Molecular Biology; Cell BiologyCCT5Pyrococcus furiosuResearch ArticlePf-CD1 Pyrococcus furiosus chaperonin subunit with the last 22 amino acids deletedBiochemistry and Biophysics Reports
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MHC class I loaded ligands from breast cancer cell lines: A potential HLA-I-typed antigen collection.

2018

Abstract To build a catalog of peptides presented by breast cancer cells, we undertook systematic MHC class I immunoprecipitation followed by elution of MHC class I-loaded peptides in breast cancer cells. We determined the sequence of 3196 MHC class I ligands representing 1921 proteins from a panel of 20 breast cancer cell lines. After removing duplicate peptides, i.e., the same peptide eluted from more than one cell line, the total number of unique peptides was 2740. Of the unique peptides eluted, more than 1750 had been previously identified, and of these, sixteen have been shown to be immunogenic. Importantly, half of these immunogenic peptides were shared between different breast cancer…

0301 basic medicineProteomicsPlant BiologyPeptideLigandsBiochemistryEpitopeAnalytical ChemistryEpitopesBreast cancerT cell-mediated immune responseHLA Antigens2.1 Biological and endogenous factorsAetiologyCancerchemistry.chemical_classificationAntigen PresentationTumorbiologyBiochemistry & Molecular BiologyBiophysicsBreast NeoplasmsArticleCell LineVaccine Related03 medical and health sciencesImmune systemBreast cancerAntigenAntigens NeoplasmCell Line TumorMHC class ImedicineGeneticsHumansAmino Acid SequenceAntigensMHC class I-restricted peptidesTumor associated antigensPreventionHistocompatibility Antigens Class ICancermedicine.diseaseHigh-Throughput Screening Assays030104 developmental biologychemistryCell cultureNeo-antigensMutationbiology.proteinCancer researchNeoplasmImmunizationBiochemistry and Cell Biology
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Lipid lowering nutraceuticals in clinical practice: position paper from an International Lipid Expert Panel.

2017

1.1. Cardiovascular disease and dyslipidemia: prevalence and global economic impact Cardiovascular diseases (CVDs) are the leading cause of mortality worldwide, reaching 31% of deaths in 2012 [1]. In particular, atherosclerosis and ischemic heart disease (IHD) are the main causes of premature death in Europe and are responsible for 42% of deaths in women and 38% in men under 75 years old [2]. The global economic impact of CVD is estimated to have been US $906 billion in 2015 and is expected to rise by 22% by 2030 [3]. Cardiovascular diseases also represent the major cause of disability in developed countries. It has been estimated that their growing burden could lead to a global increase in…

0301 basic medicineRED YEAST RICEDiseasePharmacologyPLACEBO-CONTROLLED TRIALchemistry.chemical_compound0302 clinical medicineCARDIOVASCULAR RISK-FACTORSFamily historyhealth care economics and organizationseducation.field_of_studyCONJUGATED LINOLEIC-ACIDOrvostudományokGeneral MedicinehumanitiesC-REACTIVE PROTEIN3. Good healthDENSITY-LIPOPROTEIN CHOLESTEROL030220 oncology & carcinogenesislipids (amino acids peptides and proteins)nutraceuticalLife Sciences & Biomedicineposition paperMODERATELY HYPERCHOLESTEROLEMIC SUBJECTSmedicine.medical_specialtyRANDOMIZED CONTROLLED-TRIALSeducationPopulationGuidelines/RecommendationsKlinikai orvostudományok03 medical and health sciencesMedicine General & InternallipidGeneral & Internal MedicineInternal medicineDiabetes mellitusmedicineCORONARY-HEART-DISEASERisk factoreducationFATTY LIVER-DISEASEScience & TechnologyCholesterolbusiness.industrydyslipidemia1103 Clinical Sciencesmedicine.disease030104 developmental biologychemistryrecommendationsEtiologybusinessDyslipidemiaArchives of medical science : AMS
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RepeatsDB 2.0: improved annotation, classification, search and visualization of repeat protein structures

2017

RepeatsDB 2.0 (URL: http://repeatsdb.bio.unipd.it/) is an update of the database of annotated tandem repeat protein structures. Repeat proteins are a widespread class of non-globular proteins carrying heterogeneous functions involved in several diseases. Here we provide a new version of RepeatsDB with an improved classification schema including high quality annotations for ∼5400 protein structures. RepeatsDB 2.0 features information on start and end positions for the repeat regions and units for all entries. The extensive growth of repeat unit characterization was possible by applying the novel ReUPred annotation method over the entire Protein Data Bank, with data quality is guaranteed by a…

0301 basic medicineRepetitive Sequences Amino Acid[SDV.BC]Life Sciences [q-bio]/Cellular BiologyBiologyBioinformaticsSearch engineAnnotationStructure-Activity Relationship03 medical and health sciences0302 clinical medicineTandem repeatGeneticsAnimalsHumansDatabase IssueDatabases ProteinComputingMilieux_MISCELLANEOUSRepeat unit030304 developmental biology0303 health sciencesInformation retrievalProteinscomputer.file_formatProtein Data BankVisualizationSchema (genetic algorithms)030104 developmental biologyData qualityCorrigendumcomputerSoftware030217 neurology & neurosurgeryNucleic Acids Research
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The Effect of Resveratrol on the Composition and State of Lipids and the Activity of Phospholipase A2 During the Excitation and Regeneration of Somat…

2019

It has been shown that in the somatic nerve's lipids, both during excitation and transection, changes occur with the composition of individual phospholipids and in phospholipids fatty acids, which changes the phase state of the myelin and nerve fiber axolemma lipid bilayer. A main contribution in the nerve degenerative processes is dependent on the composition phospholipid's fatty acid changes during the activation of both Ca2+-dependent and Ca2+-independent phospholipase A2 forms. At the same time, we studded changes in phosphoinisitol (PI) and diacylglycerol (DAG), which depend on the phosphoinositide cycle function during nerve excitation and degeneration processes. It was found that mye…

0301 basic medicineRhythmic excitationMyelinated nerve fiberPhysiologyPhospholipidNerve fiberresveratrollcsh:Physiology03 medical and health sciencesMyelinchemistry.chemical_compound0302 clinical medicinePhospholipase A2Physiology (medical)medicineskin and connective tissue diseasesphospholipidsDiacylglycerol kinasebiologylcsh:QP1-981Chemistrynerve intersectionmyelinated nerve fibersrhythmic excitation030104 developmental biologymedicine.anatomical_structurenervous system030220 oncology & carcinogenesisBiophysicsbiology.proteinlipids (amino acids peptides and proteins)Sciatic nervesense organsFrontiers in Physiology
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