1998
Structure−Function Relationships in Side Chain Lactam Cross-Linked Peptide Models of a Conserved N-Terminal Domain of Apolipoprotein E †
Benzinger T, Braddock D, Dominguez S, Burkoth T, Miller-Auer H, Subramanian R, Fless G, Jones D, Lynn D, Meredith S. Structure−Function Relationships in Side Chain Lactam Cross-Linked Peptide Models of a Conserved N-Terminal Domain of Apolipoprotein E †. Biochemistry 1998, 37: 13222-13229. PMID: 9748329, DOI: 10.1021/bi980482f.Peer-Reviewed Original ResearchMeSH KeywordsAmino Acid SequenceAnimalsApolipoproteins ECell LineCircular DichroismConserved SequenceEmbryo, MammalianFibroblastsIodine RadioisotopesLactamsMiceModels, MolecularMolecular Sequence DataNuclear Magnetic Resonance, BiomolecularPeptide FragmentsProtein Structure, SecondaryReceptors, LDLStructure-Activity RelationshipConceptsPeptide IVPeptide modelsConformational switchSide chain lactamLipid surfaceSide chainsBioactive peptidesStructural orderMultiple conformationsBiological activityStructure-function relationshipsLactamsAlpha-helixStrategic modificationsSecondary structureHelical segmentsPeptide IIIConformationAlpha-helical segmentsShort alpha helixCOOHHelixAntipodeStructureSolution
1996
Conformationally Specific Enhancement of Receptor-Mediated LDL Binding and Internalization by Peptide Models of a Conserved Anionic N-Terminal Domain of Human Apolipoprotein E †
Braddock D, Mercurius K, Subramanian R, Dominguez S, Davies P, Meredith S. Conformationally Specific Enhancement of Receptor-Mediated LDL Binding and Internalization by Peptide Models of a Conserved Anionic N-Terminal Domain of Human Apolipoprotein E †. Biochemistry 1996, 35: 13975-13984. PMID: 8909295, DOI: 10.1021/bi960006u.Peer-Reviewed Original ResearchAmino Acid SequenceAnimalsApolipoproteins EBinding SitesBinding, CompetitiveCell LineCell MembraneConserved SequenceHeparin LyaseHumansIn Vitro TechniquesLipoproteins, LDLLiverModels, MolecularMolecular Sequence DataPeptide FragmentsPolysaccharide-LyasesProtein BindingProtein ConformationRatsReceptors, LDL
1994
Structural and thermodynamic characterization of a bioactive peptide model of apolipoprotein E: side-chain lactam bridges to constrain the conformation.
Luo P, Braddock D, Subramanian R, Meredith S, Lynn D. Structural and thermodynamic characterization of a bioactive peptide model of apolipoprotein E: side-chain lactam bridges to constrain the conformation. Biochemistry 1994, 33: 12367-77. PMID: 7918459, DOI: 10.1021/bi00207a003.Peer-Reviewed Original ResearchConceptsSide-chain lactam bridgePeptide modelsAlpha-helical peptidesLoss of entropyModel peptidesBioactive structuresNMR dataAlpha-helical structureLactam constraintsConformational flexibilityLactam bridgeKcal/Thermodynamic characterizationAlpha-helical domainBiological activityPlasma lipoprotein clearanceUnfolded stateCell surface receptorsBiological functionsPeptidesSurface receptorsStructureResiduesCentral bendCritical role