2000
Nicotine Binding to Native and Substituted Peptides Comprising Residues 188–207 of Nicotinic Acetylcholine Receptor α1, α2, α3, α4, α5, and α7 Subunits
Lentz T. Nicotine Binding to Native and Substituted Peptides Comprising Residues 188–207 of Nicotinic Acetylcholine Receptor α1, α2, α3, α4, α5, and α7 Subunits. Biochemical And Biophysical Research Communications 2000, 268: 480-484. PMID: 10679230, DOI: 10.1006/bbrc.2000.2155.Peer-Reviewed Original ResearchConceptsNicotinic acetylcholine receptor α1Acetylcholine receptor alpha subunitNicotinic acetylcholine receptor alpha-subunitHigh affinity binding componentDifferent alpha subunitsReceptor alpha subunitNeuronal peptidesReceptor α1Alpha subunitΑ7 subunitAlpha4 subunitSignificant decreaseNicotineBinding componentSynthetic peptidesLow affinityPeptidesHigh affinity
1998
Amino Acids within Residues 181–200 of the Nicotinic Acetylcholine Receptor α1 Subunit Involved in Nicotine Binding
Lentz T, Chaturvedi V, Conti-Fine B. Amino Acids within Residues 181–200 of the Nicotinic Acetylcholine Receptor α1 Subunit Involved in Nicotine Binding. Biochemical Pharmacology 1998, 55: 341-347. PMID: 9484801, DOI: 10.1016/s0006-2952(97)00474-7.Peer-Reviewed Original ResearchConceptsNicotine bindingCys-192Cys-193Alpha1 subunitReceptor alpha1 subunitReceptor α1 subunitTyr-190Tyr-198Acetylcholine receptorsΑ1 subunitGreater reductionAsp-195Significant reductionFusion proteinPro-194Single concentrationThr-196Apparent KdAmino acidsSynthetic peptidesAsp-200Position 181Individual amino acidsResidues 181Previous studies
1993
Sodium dodecyl sulfate- and carbamylcholine-induced changes in circular dichroism spectra of acetylcholine receptor synthetic peptides
Donnelly-Roberts D, Lentz T. Sodium dodecyl sulfate- and carbamylcholine-induced changes in circular dichroism spectra of acetylcholine receptor synthetic peptides. Brain Research 1993, 19: 55-61. PMID: 8361345, DOI: 10.1016/0169-328x(93)90148-i.Peer-Reviewed Original ResearchConceptsSodium dodecyl sulfatePresence of SDSDodecyl sulfateCircular dichroism spectroscopyCritical micelle concentrationCircular dichroism spectraResidue peptideSecondary structureSynthetic peptidesDichroism spectroscopySignificant secondary structureAromatic chromophoresMicelle concentrationCircular dichroismDichroism spectraNanomolar rangeAsymmetric environmentConformational changesConformationPeptidesSulfateSpectraSpectroscopyChromophore
1991
Structure-function relationships of curaremimetic neurotoxin loop 2 and of a structurally similar segment of rabies virus glycoprotein in their interaction with the nicotinic acetylcholine receptor.
Lentz T. Structure-function relationships of curaremimetic neurotoxin loop 2 and of a structurally similar segment of rabies virus glycoprotein in their interaction with the nicotinic acetylcholine receptor. Biochemistry 1991, 30: 10949-57. PMID: 1932020, DOI: 10.1021/bi00109a020.Peer-Reviewed Original ResearchMeSH KeywordsAmino Acid SequenceAnimalsBinding, CompetitiveCell MembraneElapid VenomsElectric OrganGlycoproteinsKineticsMacromolecular SubstancesModels, StructuralMolecular Sequence DataNeurotoxinsPeptidesProtein ConformationRabies virusReceptors, NicotinicSequence Homology, Nucleic AcidTorpedoTubocurarineViral ProteinsConceptsRabies virus glycoproteinAcetylcholine receptorsVirus glycoproteinNicotinic acetylcholine receptorsTorpedo electric organ membranesElectric organ membranesD-tubocurarineToxin BReceptorsLoop 2Synthetic peptidesGlycoproteinPeptidesHigh affinityStructure-function relationshipsPhe-33GroupAcetylcholineStructural and conformational similarity between synthetic peptides of curaremimetic neurotoxins and rabies virus glycoprotein
Donnelly-Roberts D, Lentz T. Structural and conformational similarity between synthetic peptides of curaremimetic neurotoxins and rabies virus glycoprotein. Brain Research 1991, 11: 107-113. PMID: 1661807, DOI: 10.1016/0169-328x(91)90112-b.Peer-Reviewed Original ResearchConceptsLoop 2Virus glycoproteinAcetylcholine receptorsRabies virus glycoproteinBeta-sheet structureCircular dichroism spectroscopyCuraremimetic neurotoxinsAcetylcholine-binding siteSynthetic peptidesNicotinic acetylcholine receptorsDichroism spectroscopyStructural similarityConformational similarityCorresponding peptidesPolyclonal antibodiesGlycoproteinPeptides
1989
Synthetic peptides of neurotoxins and rabies virus glycoprotein behave as antagonists in a functional assay for the acetylcholine receptor.
Donnelly-Roberts D, Lentz T. Synthetic peptides of neurotoxins and rabies virus glycoprotein behave as antagonists in a functional assay for the acetylcholine receptor. Chemical Biology & Drug Design 1989, 2: 221-6. PMID: 2520759.Peer-Reviewed Original ResearchConceptsLoop 2Acetylcholine receptorsLarge macromolecular complexesVirus glycoproteinCompetitive antagonist d-tubocurarineRabies virus glycoproteinSegment interactsMacromolecular complexesSynthetic peptidesNicotinic acetylcholine receptorsBC3H-1 cellsLarge moleculesFunctional assaysShort synthetic peptidesMicromolar rangeIon transportAntagonist d-tubocurarineEffective peptideBiological effectsIC50 valuesPeptidesReceptorsGlycoproteinNeurotoxinGlycoprotein peptide
1988
Binding of alpha-bungarotoxin to synthetic peptides corresponding to residues 173-204 of the alpha subunit of Torpedo, calf, and human acetylcholine receptor and restoration of high-affinity binding by sodium dodecyl sulfate.
Wilson P, Lentz T. Binding of alpha-bungarotoxin to synthetic peptides corresponding to residues 173-204 of the alpha subunit of Torpedo, calf, and human acetylcholine receptor and restoration of high-affinity binding by sodium dodecyl sulfate. Biochemistry 1988, 27: 6667-74. PMID: 3196679, DOI: 10.1021/bi00418a004.Peer-Reviewed Original Research