Search results for "trypsin inhibitor"

showing 10 items of 31 documents

Potent Inhibitor of Human Trypsins from the Aeruginosin Family of Natural Products

2021

Funding Information: We would like to thank A. Löfhjelm and L. Saari for excellent technical assistance. This work was supported by a Sigrid Jusélius Foundation grant to H.K. and the Academy of Finland funding (321809) to T.S. We would also like to thank the Erkko Foundation and Nordforsk Nordic center of Excellency NordAqua (project number #82845) and University of Helsinki’s Doctoral Programme in Microbiology and Biotechnology funding to M.N.A. D.O.A. was supported by a postdoctoral research fellowship from the São Paulo Research Foundation (FAPESP #2018/01563-2). We thank Biocenter Kuopio for the use of their facilities for molecular modeling and MD simulations. We thank the DNA Sequenci…

Proteasesserine proteases116 Chemical sciencesproteaasiluonnontuotteet01 natural sciencesBiochemistryGenomeproteomiikkaSerine03 medical and health sciencesCell Line TumorGene clusterinhibitorsHumansIC50Genetrypsiinit030304 developmental biologyCell ProliferationinhibiittoritSerine protease0303 health sciencesBiological Productsbiologybiokemia010405 organic chemistryCell growthChemistrybioinformatiikkaGeneral MedicineArticlesseriiniproteaasi0104 chemical sciences3. Good healthsyöpäsolutBiochemistryGenes Bacterialbiology.proteinMolecular MedicineproteasessyöpätauditproteiinitTrypsin InhibitorsAzabicyclo CompoundsNodulariaAeruginosins
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Template-Directed Protein Folding into a Metastable State of Increased Activity

1995

The principal objective of this work was to distinguish between kinetic and thermodynamic reaction control in protein folding. The deleterious effects of a specific mutation on spontaneous refolding competence were analyzed for this purpose. A Bowman-Birk-type proteinase inhibitor of trypsin and chymotrypsin was selected as a double-headed model protein to facilitate the detection of functional irregularities by the use of functional assays. The parent protein spontaneously folds into a single, fully active and thermodynamically stable state in a redox buffer after reduction/denaturation. By contrast, the properties of a P'1Ser--Pro variant in the trypsin-reactive subdomain differ before an…

Protein FoldingProtein ConformationMolecular Sequence DataPopulationDNA RecombinantPhi value analysisBiochemistryDenaturation (biochemistry)Amino Acid SequenceeducationConformational isomerismTrypsin Inhibitor Bowman-Birk Soybeaneducation.field_of_studyChymotrypsinBase SequencebiologyChemistryGenetic VariationContact orderSolutionsKineticsCrystallographyModels Chemicalbiology.proteinThermodynamicsProtein foldingDownhill foldingEuropean Journal of Biochemistry
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Hybrid QconCAT-Based Targeted Absolute and Data-Independent Acquisition-Based Label-Free Quantification Enables In-Depth Proteomic Characterization o…

2021

Wheat amylase/trypsin inhibitors (ATIs) have gained significant relevance as inducers of intestinal and extra-intestinal inflammation. In this study, we present a novel hybrid data-independent acquisition (DIA) liquid chromatography-mass spectrometry (LC-MS) approach, combining QconCAT technology with short microflow LC gradients and DIA and apply the method toward the quantitative proteome analysis of ATI extracts. The presented method is fast, robust, and reproducible and provides precise QconCAT-based absolute quantification of major ATI proteins while simultaneously quantifying the proteome by label-free quantification (LFQ). We analyzed extracts of 60 varieties of common wheat grown in…

ProteomicsPlant ExtractsTrypsin inhibitorReproducibility of ResultsContext (language use)General ChemistryComputational biologyBiologyBiochemistryPlant BreedingLabel-free quantificationAmylasesProteomebiology.proteinTrypsinData-independent acquisitionBottom-up proteomicsAmylaseCommon wheatTrypsin InhibitorsTriticumJournal of Proteome Research
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Potential tolerability of ancient grains in non-celiac wheat sensitivity patients: A preliminary evaluation

2022

Background and aimsA wheat-free diet (WFD) represents the elective treatment for Non-celiac Wheat Sensitivity (NCWS) patients. Preliminary reports have shown a possible better tolerability of ancient grains in these subjects. The aim of this observational study was to evaluate the frequency of consumption of ancient grains and its correlation with clinical manifestations in NCWS patients.Methods223 NCWS patients were recruited, and their consumption of ancient grains was monitored. Participants were first administered a modified version of the Pavia/Biagi questionnaire to investigate their adherence to “modern WFD.” The appearance/exacerbation of symptoms after ingestion of ancient grains w…

Settore MED/09 - Medicina InternaGeneral MedicineAmylase-Trypsin Inhibitors (ATIs) Non-celiac Wheat Sensitivity (NCWS) ancient grains wheat free diet wheat tolerabilityFrontiers in Medicine
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Interaction of explicit solvent with hydrophobic/philic/charged residues of a protein: Residue character vs. conformational context

1998

Molecular dynamics simulations of model solutes in explicit molecular water have recently elicited novel aspects of the strong nonpair additivity of the potential of mean force (PMF) and related solvent-induced forces (SIFs) and hydration. Here we present the results of the same type of work on SIFs acting on bovine pancreatic trypsin inhibitor (BPTI) at single residue/sidechain resolution. In this system, nonpair additivity and the consequent dependence of SIFs on the protein conformational context are sufficiently strong to overturn SIFs on some individual residues, relative to expectations based on their individual characters. This finding calls for a revisitation and offers a richer and…

SolventResidue (chemistry)CrystallographyMolecular dynamicsStructural BiologyComputational chemistryChemistryA proteinProtein foldingPotential of mean forceMolecular BiologyBiochemistryBovine Pancreatic Trypsin InhibitorProteins: Structure, Function, and Genetics
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Wheat Amylase Trypsin Inhibitors as Nutritional Activators of Innate Immunity

2015

While the central role of an adaptive, T cell-mediated immune response to certain gluten peptides in celiac disease is well established, the innate immune response to wheat proteins remains less well defined. We identified wheat amylase trypsin inhibitors (ATIs), but not gluten, as major stimulators of innate immune cells (dendritic cells > macrophages > monocytes), while intestinal epithelial cells were nonresponsive. ATIs bind to and activate the CD14-MD2 toll-like receptor 4 (TLR4) complex. This activation occurs both in vitro and in vivo after oral ingestion of purified ATIs or gluten, which is usually enriched in ATIs. Wheat ATIs represent a family of up to 17 proteins with molec…

T cellBiologyMicrobiologyImmune systemImmunitymedicineAnimalsHumansImmunologic FactorsNutritional Physiological PhenomenaTriticumchemistry.chemical_classificationInnate immune systemMonocyteGastroenterologynutritional and metabolic diseasesGeneral MedicineDendritic cellAcquired immune systemGlutenImmunity Innatemedicine.anatomical_structurechemistryBiochemistryAmylasesTrypsin InhibitorsDigestive Diseases
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Conformación tridimensional y reconocimiento molecular de biopolímeros : aplicación de RMN multidimensional y desarrollo de metodología de cálculo y …

1998

El objetivo principal de la Tesis ha sido la exploración, el análisis y el perfeccionamiento de las técnicas más habituales utilizadas en la determinación de la estructura y dinámica de biopolímeros en disolución. En concreto, se han utilizado métodos teóricos y experimentales para obtener las estructuras de dos biopolímeros entre los grupos más numerosos de ellos: proteínas y ácidos nucleicos. La obtención de la estructura de una proteína de interés bioquímico por sus peculiaridades cinéticas mediante dos técnicas diferentes ha sido uno de los objetivos principales en la Tesis. La aplicación de las técnicas de modelización por homología y la realización de un análisis exhaustivo sobre los …

UNESCO::CIENCIAS DE LA VIDA::Biofísica::Otrasbovine pancreatic trypsin inhibitorestructura de ácidos nucleicosprogramas de cálculoestructura de proteínas:CIENCIAS DE LA VIDA::Biofísica::Otras [UNESCO]UNESCO::QUÍMICA::Química física:QUÍMICA::Química física [UNESCO]plaastocianinaccgcggrmn
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Proteolytic cleavage of soybean Bowman-Birk inhibitor monitored by means of high-performance capillary electrophoresis. Implications for the mechanis…

1996

The hydrolysis of the soybean Bowman-Birk inhibitor in the presence of catalytic amounts of bovine trypsin and the formation of the non-covalent enzyme-inhibitor complex with an equimolar amount of enzyme are monitored by means of high-performance capillary electrophoresis (HPCE). The inhibitor is cleaved in the trypsin-reactive and more slowly in the chymotrypsin-reactive subdomain. HPCE proves itself as the only reliable analytical tool to monitor these reactions in clear contrast to classical electrophoretic, chromatographic and enzymatic methods. The most efficient separation of the intact and the two active site cleaved forms of the inhibitor was achieved in borate buffer at pH 10.0. T…

chemistry.chemical_classificationBinding SitesChromatographybiologyChemistryHydrolysisMolecular Sequence DataBiophysicsElectrophoresis CapillaryActive siteCleavage (embryo)BiochemistryCatalysisProtein Structure TertiaryKineticsElectrophoresisHydrolysisReaction rate constantEnzymeCapillary electrophoresisBiochemistryEnzyme inhibitorbiology.proteinAmino Acid SequenceTrypsin Inhibitor Bowman-Birk SoybeanJournal of Biochemical and Biophysical Methods
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Crystal structure of the bifunctional soybean Bowman-Birk inhibitor at 0.28-nm resolution. Structural peculiarities in a folded protein conformation.

1996

The Bowman-Birk inhibitor from soybean is a small protein that contains a binary arrangement of trypsin-reactive and chymotrypsin-reactive subdomains. In this report, the crystal structure of this anticarcinogenic protein has been determined to 0.28-nm resolution by molecular replacement from crystals grown at neutral pH. The crystal structure differs from a previously determined NMR structure [Werner, M. H. & Wemmer, D. E. (1992) Biochemistry 31, 999-1010] in the relative orientation of the two enzyme-insertion loops, in some details of the main chain trace, in the presence of favourable contacts in the trypsin-insertion loop, and in the orientation of several amino acid side chains. The p…

chemistry.chemical_classificationModels MolecularMagnetic Resonance SpectroscopyStereochemistryProtein ConformationMolecular Sequence DataWaterCrystal structureCrystallography X-RayBiochemistryProtein tertiary structureProtein Structure SecondaryAmino acidCrystallographychemistry.chemical_compoundKineticsProtein structurechemistrySide chainChymotrypsinProtein foldingMolecular replacementAmino Acid SequenceBifunctionalTrypsin Inhibitor Bowman-Birk SoybeanEuropean journal of biochemistry
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Proteolytic capacity in mouse cardiac muscle following strenuous exercise

1981

Proteolytic capacity in mouse cardiac muscle was analyzed 1, 3, and 6 days after exhaustive intermittent or submaximal prolonged running. No significant changes were recorded in the activities of acid or alkaline proteases, β-glucuronidase or trypsin inhibitor. Similarly, no changes were found in the rates of acid or neutral autolysis.

medicine.medical_specialtyAutolysis (biology)ProteasesTime FactorsStrenuous exerciseTrypsin inhibitorPhysical ExertionCoronary DiseaseMiceCellular and Molecular NeuroscienceInternal medicinemedicineAnimalsskin and connective tissue diseasesMolecular BiologyPharmacologyChemistryMyocardiumCardiac muscleCell Biologymedicine.anatomical_structureEndocrinologyBiochemistryMolecular Medicinesense organsPeptide HydrolasesExperientia
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