Search results for "antimicrobial peptide"

showing 10 items of 89 documents

A peptide from human β thymosin as a platform for the development of new anti-biofilm agents for Staphylococcus spp. and Pseudomonas aeruginosa

2016

Conventional antibiotics might fail in the treatment of biofilm-associated infections causing infection recurrence and chronicity. The search for antimicrobial peptides has been performed with the aim to discover novel anti-infective agents active on pathogens in both planktonic and biofilm associated forms. The fragment 9-19 of human thymosin β4 was studied through 1 μs MD simulation. Two main conformations of the peptide were detected, both constituted by a central hydrophobic core and by the presence of peripheral charged residues suggesting a possible mechanism of interaction with two models of biological membranes, related to eukaryotic or bacterial membrane respectively. In addition, …

Models Molecular0301 basic medicineStaphylococcus aureusPhysiology030106 microbiologyAntimicrobial peptidesSettore BIO/05 - ZoologiaPeptideMicrobial Sensitivity TestsMolecular Dynamics SimulationBiologymedicine.disease_causeSettore BIO/19 - Microbiologia GeneraleApplied Microbiology and BiotechnologyMicrobiologyStructure-Activity Relationship03 medical and health sciencesAnti-Infective AgentsmedicineHumansAmino Acid SequencePeptide sequencechemistry.chemical_classificationPseudomonas aeruginosaAntimicrobial peptides Molecular dynamics Staphylococcal biofilms ThymosinBiofilmThymosinGeneral MedicineAntimicrobialSettore CHIM/08 - Chimica FarmaceuticaThymosin030104 developmental biologychemistryBiochemistrySettore CHIM/03 - Chimica Generale E InorganicaBiofilmsPseudomonas aeruginosaPeptidesAntibacterial activityBiotechnology
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Recent findings on phenoloxidase activity and antimicrobial activity of hemocyanins

2003

Models MolecularInnate immune systemMonophenol MonooxygenaseTyrosinasemedicine.medical_treatmentImmunologyAntimicrobial peptidesHemocyaninBiologyAntimicrobialMicrobiologyAnti-Infective AgentsBiochemistryHemocyaninsMetalloproteinsmedicineAnimalsArthropodsDevelopmental BiologyDevelopmental & Comparative Immunology
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Antimicrobial Peptides and Their Superior Fluorinated Analogues: Structure-Activity Relationships as Revealed by NMR Spectroscopy and MD Calculations

2010

9 pag., 6 fig, 3 tab.

Models MolecularMagnetic Resonance SpectroscopyHalogenationProtein ConformationDiffusionAntimicrobial peptidesMicrobial Sensitivity TestsMolecular Dynamics SimulationBiochemistryMicelleStructure-Activity RelationshipMolecular dynamicsantimicrobial peptidesNMR spectroscopyComputational chemistryfluorineEscherichia coliOrganic chemistryAmino Acid SequenceMolecular BiologyAqueous solutionMolecular StructureChemistryOrganic ChemistrySodium Dodecyl SulfateWaterNuclear magnetic resonance spectroscopyAntimicrobialmolecular dynamicsSolutionsMembranemembranespeptidesMolecular MedicineAntimicrobialSDS micellesOligopeptidesAntimicrobial Cationic Peptides
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Established cotton stainer gut bacterial mutualists evade regulation by host antimicrobial peptides

2019

Symbioses with microorganisms are ubiquitous in nature and confer important ecological traits to animal hosts but also require control mechanisms to ensure homeostasis of the symbiotic interactions. In addition to protecting hosts against pathogens, animal immune systems recognize, respond to, and regulate mutualists. The gut bacterial symbionts of the cotton stainer bug, Dysdercus fasciatus, elicit an immune response characterized by the upregulation of c-type lysozyme and the antimicrobial peptide pyrrhocoricin in bugs with their native gut microbiota compared to that in dysbiotic insects. In this study, we investigated the impact of the elicited antimicrobial immune response on the estab…

Nymph0106 biological sciencesAntimicrobial peptidesGut flora010603 evolutionary biology01 natural sciencesApplied Microbiology and BiotechnologyMicrobiologyHeteroptera03 medical and health sciencesImmune systemRNA interferenceInvertebrate MicrobiologyAnimalsGene SilencingSymbiosis030304 developmental biology0303 health sciencesEcologybiologyHost (biology)Effectorfungibiochemical phenomena metabolism and nutritionbiology.organism_classificationGastrointestinal MicrobiomeRNA silencingbacteriaRNA InterferenceAdaptationAntimicrobial Cationic PeptidesFood ScienceBiotechnology
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Peptidomimetics – An infinite reservoir of metal binding motifs in metabolically stable and biologically active molecules

2020

The involvement of metal ions in interactions with therapeutic peptides is inevitable. They are one of the factors able to fine-tune the biological properties of antimicrobial peptides, a promising group of drugs with one large drawback - a problematic metabolic stability. Appropriately chosen, proteolytically stable peptidomimetics seem to be a reasonable solution of the problem, and the use of D-, β-, γ-amino acids, unnatural amino acids, azapeptides, peptoids, cyclopeptides and dehydropeptides is an infinite reservoir of metal binding motifs in metabolically stable, well-designed, biologically active molecules. Below, their specific structural features, metal-chelating abilities and anti…

PeptidomimeticMetal ions in aqueous solutionAntimicrobial peptidesMetal binding sites010402 general chemistryPeptides Cyclic01 natural sciencesBiochemistryInorganic ChemistryPeptoidsHumansMoleculeAmino AcidsChelating Agentschemistry.chemical_classificationBinding SitesBacteria010405 organic chemistryMetal bindingStereoisomerismBiological activityAntimicrobialCombinatorial chemistryAnti-Bacterial Agents0104 chemical sciencesAmino acidchemistryAntimicrobial peptidesPeptidomimeticsJournal of Inorganic Biochemistry
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Inactivation of an Enveloped Virus by Immobilized Antimicrobial Peptides.

2021

Infections caused by viruses are difficult to treat due to their life cycle, which depends on the replication machinery of the respective host cells. Commonly used antiviral strategies are based upon the application of, e.g., entry inhibitors and other compounds that interfere with virus replication. Besides possible side effects, the rapid occurrence of viral resistance poses a great challenge. Antimicrobial peptides (AMPs), as a component of the innate immunity, are able to kill bacteria and fungi and, in addition, may inactivate enveloped viruses. Many AMPs exert their biological function by impairing microbial and viral membranes. As a result, membrane integrity is lost, leading to bact…

PharmacologyInnate immune systembiologyChemistryOrganic ChemistryAntimicrobial peptidesBiomedical EngineeringPharmaceutical ScienceBioengineeringbiology.organism_classificationmedicine.diseaseHemolysisMembraneViral replicationBiochemistryViral envelopemedicineViral loadBacteriaAntimicrobial PeptidesBiotechnologyBioconjugate chemistry
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Zn-Enhanced Asp-Rich Antimicrobial Peptides N-Terminal Coordination by Zn(II) and Cu(II), Which Distinguishes Cu(II) Binding to Different Peptides

2021

The antimicrobial activity of surfactant-associated anionic peptides (SAAPs), which are isolated from the ovine pulmonary surfactant and are selective against the ovine pathogen Mannheimia haemolytica, is strongly enhanced in the presence of Zn(II) ions. Both calorimetry and ITC measurements show that the unique Asp-only peptide SAAP3 (DDDDDDD) and its analogs SAAP2 (GDDDDDD) and SAAP6 (GADDDDD) have a similar micromolar affinity for Zn(II), which binds to the N-terminal amine and Asp carboxylates in a net entropically-driven process. All three peptides also bind Cu(II) with a net entropically-driven process but with higher affinity than they bind Zn(II) and coordination that involves the N…

Pore Forming Cytotoxic Proteins0301 basic medicineStereochemistryQH301-705.5Metal ions in aqueous solutionAntimicrobial peptidesPeptide010402 general chemistry01 natural sciencesArticleCatalysisInorganic Chemistry03 medical and health scienceschemistry.chemical_compoundthermodynamicsDeprotonationZn(II) and Cu(II) bioinorganic chemistryPulmonary surfactantAmidePhysical and Theoretical ChemistryBiology (General)Mannheimia haemolyticaMolecular BiologyQD1-999Spectroscopychemistry.chemical_classificationOrganic ChemistryElectron Spin Resonance SpectroscopyGeneral Medicine0104 chemical sciencesComputer Science ApplicationsZincChemistry030104 developmental biologyMembranechemistryAmine gas treatingmetal-antimicrobial peptide interactionsPeptidesCopperInternational Journal of Molecular Sciences
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A lipocentric view of peptide-induced pores

2010

Although lipid membranes serve as effective sealing barriers for the passage of most polar solutes, nonmediated leakage is not completely improbable. A high activation energy normally keeps unassisted bilayer permeation at a very low frequency, but lipids are able to self-organize as pores even in peptide-free and protein-free membranes. The probability of leakage phenomena increases under conditions such as phase coexistence, external stress or perturbation associated to binding of nonlipidic molecules. Here, we argue that pore formation can be viewed as an intrinsic property of lipid bilayers, with strong similarities in the structure and mechanism between pores formed with participation …

Pore Forming Cytotoxic ProteinsCell Membrane PermeabilityMembrane permeabilityMembrane lipidsPore energeticsBiophysicsThermal fluctuationsReviewMolecular Dynamics SimulationSurface tensionMembrane LipidsAnti-Infective AgentsLipid bilayerChemistryBilayerLipidic poreGeneral MedicinePermeationCrystallographyMembrane permeabilityMembraneBiophysicsAntimicrobial peptidePore structurePorosityPore-forming proteinsEuropean Biophysics Journal
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Antilisterial peptides from Spanish dry-cured hams: Purification and identification.

2016

The typical Spanish dry-cured ham has a particular sensory quality that makes it a distinctive food, highly appreciated for consumers worldwide. Its particular physicochemical properties, such as high salt content and reduced water activity contribute to their shelf-stability. However, post-processing actions carried out for the commercialization of these products such as slicing may increase the risk of development of pathogenic microorganisms as Listeria monocytogenes. During ripening, muscle proteins are hydrolyzed by muscle peptidases releasing peptides and free amino acids. Some of these peptides have been described to exert biological activities such as antioxidant and ACE-inhibition.…

ProteomicsAntioxidantWater activitySwinemedicine.medical_treatmentAntimicrobial peptidesMicrobial Sensitivity Testsmedicine.disease_causeProteomics01 natural sciencesMicrobiologyPentapeptide repeatMass SpectrometryHydrolysis0404 agricultural biotechnologyDry-cured hamListeria monocytogenesTandem Mass SpectrometryFood PreservedmedicineEthnicityAnimalsHumansAmino Acid Sequence2. Zero hungerMass spectrometryChemistry010401 analytical chemistryRipening04 agricultural and veterinary sciences040401 food scienceListeria monocytogenes0104 chemical sciencesAnti-Bacterial AgentsMeat ProductsBiochemistrySpainAntimicrobial peptidesPeptidomimeticsPeptidesFood ScienceFood microbiology
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The conservation and diversity of ascidian cells and molecules involved in the inflammatory reaction: The Ciona robusta model

2021

Ascidians are marine invertebrate chordates belonging to the earliest branch (Tunicata) in the chordate phylum, therefore, they are of interest for studying the evolution of immune systems. Due to the known genome, the non-colonial Ciona robusta, previously considered to be C. intestinalis type A, is a model species for the study of inflammatory response. The internal defense of ascidians mainly relies on hemocytes circulating in the hemolymph and pharynx. Hemocytes can be in vivo challenged by LPS injection and various granulocyte and vacuolated cell populations differentiated to produce and release inflammatory factors. Molecular biology and gene expression studies revealed complex defens…

Regulation of gene expressionLipopolysaccharidesHemocytesAntimicrobial peptidesSettore BIO/05 - ZoologiaCollectinAscidians Ciona robusta Gene expression Immunocytes In situ hybridization Inflammation Animals Antimicrobial Peptides Hemocytes Lipopolysaccharides Phylogeny Ciona intestinalisChordateGeneral MedicineAquatic ScienceBiologybiology.organism_classificationCell biologyCiona intestinalisAscidians Ciona robusta; Inflammation; Immunocytes; In situ hybridization; Gene ExpressionHemolymphEnvironmental ChemistryGene familyAnimalsGeneAntimicrobial PeptidesPhylogenyGalectin
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