Search results for "Peptide Library"

showing 10 items of 38 documents

Developments in the use of baculoviruses for the surface display of complex eukaryotic proteins

2001

The ability to couple genotype to phenotype has proven to be of immense value in systems such as phage display and has allowed genes encoding novel functions to be selected directly from complex libraries. However, the complexity of many eukaryotic proteins places a severe constraint on successful display in Escherichia coli. This restriction could be resolved if a eukaryotic virus could be similarly engineered for display purposes. Preliminary data have suggested that the baculovirus Autographa californica, a multiple nuclear polyhedrosis virus (AcMNPV) is a candidate for eukaryotic virus display because the insertion of peptides into the native virus coat protein, or the expression of for…

InsectaPhage displayExpression vectorbiologyvirusesGene Transfer TechniquesVirionBioengineeringGenome ViralComputational biologybiology.organism_classificationVirologyFusion proteinVirusAutographa californicaPeptide LibraryAnimalsCloning MolecularGenetic EngineeringPeptide libraryBaculoviridaeViral Fusion ProteinsGeneFunctional genomicsBiotechnologyTrends in Biotechnology
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Identification from a Positional Scanning Peptoid Library of in Vivo Active Compounds That Neutralize Bacterial Endotoxins

2005

4 pages, 3 figures, 1 table.-- PMID: 15715495 [PubMed].-- Printed version published Feb 24, 2005.-- Supporting information available at: http://pubs.acs.org/doi/suppl/10.1021/jm040834i

LipopolysaccharidesGram-negative bacteriaDatabases FactualLipopolysaccharideStereochemistryLipopolysaccharide (LPS)Peptidemedicine.disease_causeLipid AMiceVivo active compoundsPeptoidschemistry.chemical_compoundIn vivoGram-Negative BacteriaDrug DiscoverymedicineAnimalsPositional scanning peptoid libraryPeptide librarychemistry.chemical_classificationbiologyTumor Necrosis Factor-alphaToxinPeptoidbiology.organism_classificationLipid ABiochemistrychemistryMolecular Medicinelipids (amino acids peptides and proteins)Journal of Medicinal Chemistry
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Evaluation of T7 and lambda phage display systems for survey of autoantibody profiles in cancer patients.

2008

In the current study we attempted to evaluate the suitability of T7 Select 10-3b and lambdaKM8 phage display systems for the identification of antigens eliciting B cell responses in cancer patients and the production of phage-displayed antigen microarrays that could be exploited for the monitoring of autoantibody profiles. Members of 15 tumour-associated antigen (TAA) families were cloned into both phage display vectors and the TAA mini-libraries were immunoscreened with 22 melanoma patients' sera resulting in the detection of reactivity against members of 5 antigen families in both systems, yet with variable sensitivity. T7 phage display system showed greater sensitivity for the detection …

Melanoma-associated antigenPhage displayMicroarrayT7 phageAntibodies NeoplasmImmunologyAutoantibodyProtein Array AnalysisBiologybiology.organism_classificationVirologyMolecular biologyBacteriophage lambdaBacteriophageAntigenAntigens NeoplasmPeptide LibraryBacteriophage T7Immunology and AllergyHumansGenomic libraryCloning MolecularMelanomaAutoantibodiesGene LibraryJournal of immunological methods
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Combinatorial approaches: A new tool to search for highly structured β-hairpin peptides

2002

Here we present a combinatorial approach to evolve a stable β-hairpin fold in a linear peptide. Starting with a de novo -designed linear peptide that shows a β-hairpin structure population of around 30%, we selected four positions to build up a combinatorial library of 20 4 sequences. Deconvolution of the library using circular dichroism reduced such a sequence complexity to 36 defined sequences. Circular dichroism and NMR of these peptides resulted in the identification of two linear 14-aa-long peptides that in plain buffered solutions showed a percentage of β-hairpin structure higher than 70%. Our results show how combinatorial approaches can be used to obtain highly structured peptide s…

Models MolecularProtein FoldingCircular dichroismMagnetic Resonance SpectroscopyFold (higher-order function)Molecular Sequence DataPopulationPeptideComputational biologyBiologyProtein Structure SecondaryPeptide LibraryCombinatorial Chemistry TechniquesAmino Acid Sequenceeducationchemistry.chemical_classificationeducation.field_of_studyMultidisciplinaryCircular DichroismBiological SciencesCombinatorial chemistryTemplatechemistryDrug DesignDeconvolutionPeptidesProceedings of the National Academy of Sciences
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Proteomic identification of protease cleavage sites characterizes prime and non-prime specificity of cysteine cathepsins B, L, and S.

2011

Cysteine cathepsins mediate proteome homeostasis and have pivotal functions in diseases such as cancer. To better understand substrate recognition by cathepsins B, L, and S, we applied proteomic identification of protease cleavage sites (PICS) for simultaneous profiling of prime and non-prime specificity. PICS profiling of cathepsin B endopeptidase specificity highlights strong selectivity for glycine in P3' due to an occluding loop blocking access to the primed subsites. In P1', cathepsin B has a partial preference for phenylalanine, which is not found for cathepsins L and S. Occurrence of P1' phenylalanine often coincides with aromatic residues in P2. For cathepsin L, PICS identifies 845 …

Models MolecularProteomicsTime Factorsmedicine.medical_treatmentProteolysisCathepsin LPhenylalanineGlycineBiologyBiochemistryCathepsin BPichiaCathepsin BSubstrate SpecificityCathepsin LCathepsin OPeptide LibraryCatalytic DomainmedicineHumansCathepsin SEnzyme AssaysCathepsinProteasemedicine.diagnostic_testGeneral ChemistryHydrogen-Ion ConcentrationMolecular biologyCathepsinsHEK293 CellsBiochemistryProteolysisbiology.proteinCysteinePeptide HydrolasesProtein BindingJournal of proteome research
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Identification of SNARE complex modulators that inhibit exocytosis from an alpha-helix-constrained combinatorial library.

2003

Synthetic peptides patterned after the proteins involved in vesicle fusion [the so-called SNARE (soluble N-ethylmaleimide-sensitive fusion protein attachment protein receptor) proteins] are potent inhibitors of SNARE complex assembly and neuronal exocytosis. It is noteworthy that the identification of peptide sequences not related to the SNARE proteins has not been accomplished yet; this is due, in part, to the structural constraints and the specificity of the protein interactions that govern the formation of the SNARE complex. Here we have addressed this question and used a combinatorial approach to identify peptides that modulate the assembly of the SNARE core complex and inhibit neuronal…

Models MolecularVesicle fusionMacromolecular SubstancesChromaffin CellsMolecular Sequence DataVesicular Transport ProteinsBiologyBiochemistryExocytosisExocytosisProtein Structure SecondaryPeptide LibraryAnimalsAmino Acid SequencePeptide libraryMolecular BiologyCells CulturedSNARE complex assemblyNeuronsSTX1AMembrane ProteinsMunc-18Cell BiologyFusion proteinCell biologyRatsCattleSNARE complexPeptidesSNARE ProteinsResearch ArticleThe Biochemical journal
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Small molecule inhibitors of Apaf-1-related caspase- 3/-9 activation that control mitochondrial-dependent apoptosis

2006

10 pages, 5 figures.-- PMID: 16341125 [PubMed].-- Available online Dec 9, 2005.

Multiprotein complexCytochromeProtein-protein interactionsApoptosisCaspase 3MitochondrionLigandsCell LineChemical librarychemistry.chemical_compoundPeptide LibraryApoptosomesPeptoidHumansCombinatorial libraries inhibitorApoptosomeProtein PrecursorsMolecular BiologybiologyCaspase 3Intrinsic apoptosisCytochromes cCell BiologyCaspase InhibitorsCaspase 9Recombinant ProteinsMitochondriaCell biologyEnzyme ActivationCaspasa-9Apoptotic Protease-Activating Factor 1chemistryBiochemistryN-substituted GlycinesApoptosisCaspasa-3biology.proteinApoptosomeApaf-1Molecular recognitionSmall moleculeProtein BindingCell Death & Differentiation
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The Putative Natural Killer Decoy Early Genem04(gp34) of Murine Cytomegalovirus Encodes an Antigenic Peptide Recognized by Protective Antiviral CD8 T…

2000

ABSTRACTSeveral early genes of murine cytomegalovirus (MCMV) encode proteins that mediate immune evasion by interference with the major histocompatibility complex class I (MHC-I) pathway of antigen presentation to cytolytic T lymphocytes (CTL). Specifically, them152gene product gp37/40 causes retention of MHC-I molecules in the endoplasmic reticulum (ER)-Golgi intermediate compartment. Lack of MHC-I on the cell surface should activate natural killer (NK) cells recognizing the “missing self.” The retention, however, is counteracted by them04early gene product gp34, which binds to folded MHC-I molecules in the ER and directs the complex to the cell surface. It was thus speculated that gp34 mi…

MuromegalovirusGenes ViralImmunologyAntigen presentationchemical and pharmacologic phenomenaGenome ViralCD8-Positive T-LymphocytesMajor histocompatibility complexMicrobiologyImmediate-Early ProteinsGene productMiceViral ProteinsImmune systemAntigenPeptide LibraryVirologyAnimalsCytotoxic T cellHistocompatibility Antigen H-2DAntigens ViralCells CulturedGlycoproteinsMice Inbred BALB CMembrane GlycoproteinsbiologyHistocompatibility Antigens Class IH-2 AntigensVirologyKiller Cells NaturalCTL*Insect Sciencebiology.proteinPathogenesis and ImmunityFemaleCarrier ProteinsPeptidesCD8T-Lymphocytes CytotoxicJournal of Virology
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A positional scanning combinatorial library of peptoids as a source of biological active molecules: identification of antimicrobials

2003

9 pages, 4 figures, 2 schemes, 3 tables.-- PMID: 12959560 [PubMed].-- Printed version published in issue Sep-Oct 2003.-- Supporting information available at: http://pubs.acs.org/doi/suppl/10.1021/cc020075u

N-alkylglycineStereochemistryChemistryPositional scanning libraryMicrobial Sensitivity TestsGeneral ChemistryAntimicrobial activityAntimicrobialCombinatorial chemistryAnti-Bacterial AgentsPeptoidsPeptide LibraryChemical diversityCombinatorial Chemistry TechniquesMoleculeIdentification (biology)
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Enhanced baculovirus-mediated transduction of human cancer cells by tumor-homing peptides.

2006

ABSTRACT Tumor cells and vasculature offer specific targets for the selective delivery of therapeutic genes. To achieve tumor-specific gene transfer, baculovirus tropism was manipulated by viral envelope modification using baculovirus display technology. LyP-1, F3, and CGKRK tumor-homing peptides, originally identified by in vivo screening of phage display libraries, were fused to the transmembrane anchor of vesicular stomatitis virus G protein and displayed on the baculoviral surface. The fusion proteins were successfully incorporated into budded virions, which showed two- to fivefold-improved binding to human breast carcinoma (MDA-MB-435) and hepatocarcinoma (HepG2) cells. The LyP-1 pepti…

Phage displayCarcinoma HepatocellularTransgenevirusesImmunologyBreast NeoplasmsGene deliveryMicrobiologyVesicular stomatitis Indiana virusTransduction (genetics)Gene DeliveryViral envelopePeptide LibraryTransduction GeneticVirologyCell Line TumorHumansGlycoproteinsbiologyGenetic Therapybiology.organism_classificationMolecular biologyFusion proteinNeoplasm ProteinsVesicular stomatitis virusCell cultureInsect ScienceCapsid ProteinsPeptidesBaculoviridaeProtein BindingJournal of virology
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