0000000000353758

AUTHOR

Puig Mora

showing 5 related works from this author

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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Tiratricol neutralizes bacterial endotoxins and reduces lipopolysaccharide-induced TNF-alpha production in the cell.

2008

Contains fulltext : 70610.pdf (Publisher’s version ) (Closed access) The screening of a commercially available library of compounds has proved a successful strategy for the identification of a lead compound in a drug discovery programme. Here, we analysed 880 off-patent drugs, which initially comprised the Prestwick Chemical library, as sources of bacterial endotoxin neutralizers. We identified 3,3',5-triiodo-thyroacetic acid (tiratricol) as a non-antibacterial compound that neutralizes the toxic lipopolysaccharide.

LipopolysaccharidesendotoxinLipopolysaccharideCelllipopolysaccharide-antagonistsBiology:Enginyeria dels materials [Àrees temàtiques de la UPC]BiochemistryCell LineChemical libraryMicrobiologyLipid ASepsissepsisMiceStructure-Activity Relationshipchemistry.chemical_compoundtumour necrosis factor-alphaDrug DiscoveryEscherichia colimedicineAnimalsDrugs--Designlipid APharmacologyTriiodothyroacetic acidMedicaments -- DissenyTumor Necrosis Factor-alphaDrug discoveryOrganic Chemistrylipopolysaccharidetumour necrosis factor-amedicine.diseaseAnti-Bacterial AgentsEndotoxinsmedicine.anatomical_structurechemistryTriiodothyronineMolecular Medicineseptic shockLead compoundImmunity infection and tissue repair [NCMLS 1]
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Roles of a conserved proline in the internal fusion peptide of Ebola glycoprotein

2004

AbstractThe structural determinants underlying the functionality of viral internal fusion peptides (IFPs) are not well understood. We have compared EBOwt (GAAIGLAWIPYFGPAAE), representing the IFP of the Ebola fusion protein GP, and EBOmut (GAAIGLAWIPYFGRAAE) derived from a non-functional mutant with conserved Pro537 substituted by Arg. P537R substitution did not abrogate peptide-membrane association, but interfered with the ability to induce bilayer destabilization. Structural determinations suggest that Pro537 is required to preserve a membrane-perturbing local conformation in apolar environments.

Circular dichroismEbola glycoproteinProtein insertion into membranesProlinePeptide conformationMutantMolecular Sequence DataBiophysicsBiochemistrySendai viruschemistry.chemical_compoundStructural BiologyGeneticsProlineAmino Acid SequenceMolecular BiologyPeptide sequencePOPCchemistry.chemical_classificationChemistryProteïnes de membranaCell BiologyEbolavirusFusion proteinPeptide FragmentsPeptide ConformationViral fusion peptideBiochemistryAvian Sarcoma VirusesLiposomesHIV-1PèptidsGlycoproteinPeptide–lipid interactionViral Fusion ProteinsFEBS Letters
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Design of bioactive and structurally well-defined peptides from conformationally restricted libraries

2004

Libraries of peptides and proteins can be categorized according to the function of their origin in gene- and synthetic-based libraries. Both kinds of libraries have the potential to generate the same grade of molecular diversity, although the limits imposed by the synthetic methods have been lately a matter of discussion. However, the use of synthetic strategies allows incorporation of non-natural amino acids. The development of canfonnallonally restricted synthetic peptide libraries can be considered as a point of convergence of the two methodologies. In these libraries the diversity is grafted into scaffolds that are defined by stable secondary structural motifs, and the deconvolution pro…

chemistry.chemical_classificationPeptidomimeticStereochemistryOrganic ChemistryProtein domainBiophysicsPeptideGeneral MedicineComputational biologyBiochemistryAmino acidBiomaterialsFolding (chemistry)chemistryWell-definedStructural motifFunction (biology)Biopolymers
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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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