Search results for "PEPTIDE"

showing 10 items of 4589 documents

Biomedical Applications of Polylactide (PLA) and Its Copolymers.

2018

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Anti-Infective AgentPolyestersMicrofluidicsPolyesterPharmaceutical ScienceBiocompatible Materials02 engineering and technology01 natural sciencesAnalytical ChemistryPolymerizationlcsh:QD241-441Nanoparticlelcsh:Organic chemistryAnti-Infective AgentsDrug DiscoveryCopolymerHumansPhysical and Theoretical ChemistryDrug CarrierBiocompatible MaterialDrug CarriersPolymer scienceTissue Scaffolds010405 organic chemistryChemistryOrganic Chemistry021001 nanoscience & nanotechnologyBone Diseases Infectious0104 chemical sciencesBone Diseases Infectioun/aEditorialMicrofluidicChemistry (miscellaneous)PeptideMolecular MedicineNanoparticles0210 nano-technologyPeptidesHumanMolecules (Basel, Switzerland)
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Echinoderm Antimicrobial Peptides: The Ancient Arms of the Deuterostome Innate Immune System

2016

Antimicrobial peptides (AMPs) are widely expressed in organisms and have been linked to innate and acquired immunity in vertebrates. These compounds are constitutively expressed from different cellular types to interact directly with infectious agents and/or modulate immunoreactions. In invertebrates, including echinoderms, which lack a vertebrate-type adaptive immune system, AMPs represent the major humoral defense system against infection, showing a diverse spectrum of action mechanisms, most of them related to plasma membrane disturbance and lethal alteration of microbial integrity. Here, we summarize the knowledge of AMPs in echinoderms as Strongylocins identified in the sea urchins, St…

Antibiofilm peptideInnate immunityEchinodermImmunology and Microbiology (all)BiofilmMedicine (all)Settore BIO/05 - ZoologiaAntimicrobial peptideSettore BIO/19 - Microbiologia Generale
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FRAGMENTS OF BETA-THYMOSIN FROM THE SEA-URCHIN PARACENTROTUS LIVIDUS AS NOVEL ANTIMICROBIAL PEPTIDES AGAINST STAPHYLOCOCCAL BIOFILMS

2012

With the aim to face the threat of pathogen biofilms intrinsically resistant to conventional antibiotics, we focused on coelomocytes, the immune mediators in echinoderms, as source of novel antimicrobial peptides (AMPs). The proteic fraction <5kDa from coelomocytes cytosol of the sea-urchin Paracentrotus lividus (5-CC) was tested against a group of Gram positive and Gram negative pathogen reference strains. The 5-CC of P. lividus resulted active against all tested strains at concentrations ranging from 15.8 to 253.7 mg/mL. The ability to prevent staphylococcal biofilm formation was evaluated against the biofilm of clinical strain S.epidermidis 1457 using live/dead staining in combination wi…

Antibiotic resistanceBiofilmAntimicrobial peptidesSettore BIO/19 - Microbiologia GeneraleStaphylococci
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Antibody Induction Directed against the Tumor-Associated MUC4 Glycoprotein

2015

Mucin glycoproteins are important diagnostic and therapeutic targets for cancer treatment. Although several strategies have been developed to explore anti-tumor vaccines based on MUC1 glycopeptides, only few studies have focused on vaccines directed against the tumor-associated MUC4 glycoprotein. MUC4 is an important tumor marker overexpressed in lung cancer and uniquely expressed in pancreatic ductual adenocarcinoma. The aberrant glycosylation of MUC4 in tumor cells results in an exposure of its peptide backbone and the formation of tumor-associated glycopeptide antigens. Due to the low immunogenicity of these endogenous structures, their conjugation with immune stimulating peptide or prot…

Antibodies NeoplasmMolecular Sequence DataCancer VaccinesBiochemistryEpitopeEpitopesMiceAntigenAntibody SpecificityCell Line TumorTetanus ToxoidAnimalsHumansAmino Acid SequenceMolecular BiologyMUC1chemistry.chemical_classificationMice Inbred BALB CMucin-4biologyImmune SeraImmunogenicityVaccinationOrganic ChemistryToxoidGlycopeptidePancreatic NeoplasmschemistryTandem Repeat SequencesImmunologybiology.proteinMolecular MedicineFemalesense organsAntibodyGlycoproteinChemBioChem
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Antibody Complementarity-Determining Regions (CDRs) Can Display Differential Antimicrobial, Antiviral and Antitumor Activities

2008

9 p. Background: Complementarity-determining regions (CDRs) are immunoglobulin (Ig) hypervariable domains that determine specific antibody (Ab) binding. We have shown that synthetic CDR-related peptides and many decapeptides spanning the variable region of a recombinant yeast killer toxin-like antiidiotypic Ab are candidacidal in vitro. An alanine-substituted decapeptide from the variable region of this Ab displayed increased cytotoxicity in vitro and/or therapeutic effects in vivo against various bacteria, fungi, protozoa and viruses. The possibility that isolated CDRs, represented by short synthetic peptides, may display antimicrobial, antiviral and antitumor activities irrespective of Ab…

Antifungal AgentsBIOCHEMISTRY AND MOLECULAR BIOLOGYMolecular Sequence DataImmunologylcsh:MedicineAntineoplastic AgentsMicrobial Sensitivity TestsComplementarity determining regionBiologyAntiviral AgentsOncology/Skin CancersAntibodiesMiceMicrobiology/Applied MicrobiologyAntigenBiochemistry/Protein ChemistryInfectious Diseases/Fungal InfectionsIn vivoCell Line TumorCandida albicansInfectious Diseases/Viral InfectionsAnimalsHumansAmino Acid Sequencelcsh:SciencePeptide sequenceMultidisciplinaryMEDICINElcsh:RAntimicrobialComplementarity Determining RegionsVirologyIn vitroOncologyBiochemistryViral replicationAGRICULTURAL AND BIOLOGICAL SCIENCESVirology/Immunodeficiency VirusesHIV-1biology.proteinlcsh:QAntibodyResearch ArticlePLoS ONE
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Synthesis and biological evaluation of abietic acid derivatives

2009

A series of C18-oxygenated derivatives of abietic acid were synthesized and evaluated for their cytotoxic, antimycotic, and antiviral activities. In general, the introduction of an aldehyde group at C18 did improve the resultant bioactivity, while the presence of an acid or alcohol led to less active compounds.

Antifungal AgentsCarboxylic acidMolecular ConformationAntineoplastic AgentsAlcoholHerpesvirus 1 HumanMicrobial Sensitivity TestsPrimary alcoholAntiviral AgentsChemical synthesisAldehydeStructure-Activity Relationshipchemistry.chemical_compoundChlorocebus aethiopsDrug DiscoveryAnimalsHumansStructure–activity relationshipOrganic chemistryAbietic acidVero CellsCandidaCell ProliferationPharmacologychemistry.chemical_classificationDose-Response Relationship DrugAspergillus fumigatusOrganic Chemistryfood and beveragesStereoisomerismGeneral Medicineequipment and suppliesAspergilluschemistryDrug DesignAbietaneslipids (amino acids peptides and proteins)DiterpeneHeLa CellsEuropean Journal of Medicinal Chemistry
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Peptides of the Constant Region of Antibodies Display Fungicidal Activity

2012

Synthetic peptides with sequences identical to fragments of the constant region of different classes (IgG, IgM, IgA) of antibodies (Fc-peptides) exerted a fungicidal activity in vitro against pathogenic yeasts, such as Candida albicans, Candida glabrata, Cryptococcus neoformans, and Malassezia furfur, including caspofungin and triazole resistant strains. Alanine-substituted derivatives of fungicidal Fc-peptides, tested to evaluate the critical role of each residue, displayed unaltered, increased or decreased candidacidal activity in vitro. An Fc-peptide, included in all human IgGs, displayed a therapeutic effect against experimental mucosal and systemic candidiasis in mouse models. It is in…

Antifungal AgentsErythrocyteslcsh:MedicineImmunoglobulin Gchemistry.chemical_compoundEchinocandinsMiceCaspofunginCandida albicanslcsh:ScienceCandida albicansMice Inbred BALB CMultidisciplinarybiologyCandidiasisAnimal ModelsInfectious DiseasesMedicineFemaleMalasseziaImmunoglobulin Constant RegionsResearch ArticleImmunologyMycologyMicrobial Sensitivity TestsMicrobiologyHemolysisAntibodiesMicrobiologyLipopeptidesImmune systemModel OrganismsDrug Resistance FungalmedicineAnimalsHumansBiologyCryptococcus neoformansMalasseziaCandida glabratalcsh:RImmunityTriazolesbiology.organism_classificationmedicine.diseaseImmunoglobulin ADisease Models AnimalchemistryImmunoglobulin MImmunoglobulin Gbiology.proteinCryptococcus neoformanslcsh:QSystemic candidiasisCaspofunginPeptidesPLoS ONE
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Alternative Biosynthetic Starter Units Enhance the Structural Diversity of Cyanobacterial Lipopeptides

2019

Puwainaphycins (PUWs) and minutissamides (MINs) are structurally analogous cyclic lipopeptides possessing cytotoxic activity. Both types of compound exhibit high structural variability, particularly in the fatty acid (FA) moiety. Although a biosynthetic gene cluster responsible for synthesis of several PUW variants has been proposed in a cyanobacterial strain, the genetic background for MINs remains unexplored. Herein, we report PUW/MIN biosynthetic gene clusters and structural variants from six cyanobacterial strains. Comparison of biosynthetic gene clusters indicates a common origin of the PUW/MIN hybrid nonribosomal peptide synthetase and polyketide synthase. Surprisingly, the biosynthet…

Antifungal AgentsGenetics and Molecular BiologyCyanobacteria01 natural sciencesApplied Microbiology and BiotechnologycyanobacteriaPeptides Cyclicbiosynteesi03 medical and health scienceschemistry.chemical_compoundLipopeptidesBiosynthesisAnti-Infective AgentsBacterial ProteinsNonribosomal peptidePolyketide synthaseGene clusterPeptide SynthasessyanobakteeritGene030304 developmental biology2. Zero hungerchemistry.chemical_classification0303 health sciencesNatural productEcologybiology010405 organic chemistryLipopeptideAnabaenaYeast0104 chemical scienceschemistryBiochemistrypeptiditGenes BacterialMultigene Familybiology.proteinpeptidesbiosynthesisPolyketide SynthasesFood ScienceBiotechnology
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Isolation and characterization of Saccharomyces cerevisiae mutants resistant to aculeacin A

1991

Aculeacin A is a lipopeptide that inhibits beta-glucan synthesis in yeasts. A number of Saccharomyces cerevisiae mutants resistant to this antibiotic were isolated, and four loci (ACR1, ACR2, ACR3, and ACR4) whose products are involved in the sensitivity to aculeacin A of yeast cells were defined. Mutants containing mutations in the four loci were also resistant to echinocandin B, another member of this lipopeptide family of antibiotics. In contrast, acr1, acr3, and acr4 mutants were resistant to papulacandin B (an antibiotic containing a disaccharide linked to two fatty acid chains that also inhibits beta-glucan synthesis), but acr2 mutants were susceptible to this antibiotic. This result …

Antifungal AgentsLlevat de cervesaGenotypeMutantSaccharomyces cerevisiaePapulacandin BSaccharomyces cerevisiaemedicine.disease_causePeptides CyclicMicrobiologyFungal ProteinsEchinocandinschemistry.chemical_compoundCell WallEchinocandin BmedicinePharmacology (medical)PharmacologyFungal proteinMutationbiologyMutagenicity TestsMembrane ProteinsLipopeptideAminoglicòsidbiology.organism_classificationYeastAnti-Bacterial AgentsAminoglucòsidsAminoglycosidesInfectious DiseaseschemistryBiochemistryGlucosyltransferasesMutationSchizosaccharomyces pombe ProteinsPeptidesResearch Article
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Identification of Novel Hexapeptides Bioactive against Phytopathogenic Fungi through Screening of a Synthetic Peptide Combinatorial Library

2002

The purpose of the present study was to improve the antifungal activity against selected phytopathogenic fungi of the previously identified hexapeptide PAF19. We describe some properties of a set of novel synthetic hexapeptides whose D-amino acid sequences were obtained through screening of a synthetic peptide combinatorial library in a positional scanning format. As a result of the screening, 12 putative bioactive peptides were identified, synthesized, and assayed. The peptides PAF26 (Ac-rkkwfw-NH(2)), PAF32 (Ac-rkwhfw-NH(2)), and PAF34 (Ac-rkwlfw-NH(2)) showed stronger activity than PAF19 against isolates of Penicillium digitatum, Penicillium italicum, and Botrytis cinerea. PAF26 and PAF3…

Antifungal AgentsMicrobial Sensitivity TestsApplied Microbiology and BiotechnologyMelittinPenicillium italicumMicrobiologyAntifungal peptidechemistry.chemical_compoundFusariumPeptide LibraryFusarium oxysporummedicineEnzymology and Protein EngineeringPeptide libraryPhytopathogenic fungiPlant DiseasesBotrytis cinereaPenicillium digitatumEcologybiologyPenicilliumfood and beveragesBiological activitybiology.organism_classificationmedicine.drug_formulation_ingredientBiochemistrychemistryPenicillium expansumPeptidesOligopeptidesHexapeptide PAF19Food ScienceBiotechnology
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