2025
Drugging Disordered Proteins by Conformational Selection to Inform Therapeutic Intervention
Bogin B, Levine Z. Drugging Disordered Proteins by Conformational Selection to Inform Therapeutic Intervention. Journal Of Chemical Theory And Computation 2025, 21: 3204-3215. PMID: 40029731, DOI: 10.1021/acs.jctc.4c01160.Peer-Reviewed Original ResearchConceptsIslet amyloid polypeptideIntrinsically disordered proteinsConformational selectionDisordered proteinsHuman islet amyloid polypeptideMolecular dynamics simulationsStable binding sitesSelf-assembling sequencesIAPP sequenceFixed conformationAmyloid polypeptideUmbrella samplingBinding preferencesConformational specificityTwo-state modelDynamics simulationsConformational heterogeneityNew conformationsBinding sitesMolecular binding mechanismsConformationBinding mechanismFoldamersStructural conformationProtein
2013
Membrane Permeation Induced by Aggregates of Human Islet Amyloid Polypeptides
Poojari C, Xiao D, Batista V, Strodel B. Membrane Permeation Induced by Aggregates of Human Islet Amyloid Polypeptides. Biophysical Journal 2013, 105: 2323-2332. PMID: 24268144, PMCID: PMC3838749, DOI: 10.1016/j.bpj.2013.09.045.Peer-Reviewed Original ResearchConceptsChiral sum frequency generation (SFG) spectroscopySum frequency generation spectroscopyMembrane/water interfaceFrequency generation spectroscopyΒ-sheet secondary structureChannel-forming proteinMolecular dynamics simulationsSimulated SFG spectraAmphiphilic propertiesHuman islet amyloidGeneration spectroscopySFG spectraWater interfaceΒ-sandwichHuman islet amyloid polypeptideIslet β-cellsAmyloid polypeptideWater permeationDynamics simulationsHIAPP aggregatesSecondary structureMembrane permeationIslet amyloid polypeptideΒ-cellsFibrillar structures
2011
Amphiphilic Adsorption of Human Islet Amyloid Polypeptide Aggregates to Lipid/Aqueous Interfaces
Xiao D, Fu L, Liu J, Batista V, Yan E. Amphiphilic Adsorption of Human Islet Amyloid Polypeptide Aggregates to Lipid/Aqueous Interfaces. Journal Of Molecular Biology 2011, 421: 537-547. PMID: 22210153, PMCID: PMC3350761, DOI: 10.1016/j.jmb.2011.12.035.Peer-Reviewed Original ResearchConceptsLipid/aqueous interfaceAqueous interfaceΒ-sheet aggregatesAb initio quantum chemistry calculationsChiral sum frequency generation (SFG) spectroscopySum frequency generation spectroscopyQuantum chemistry calculationsFrequency generation spectroscopyHuman islet amyloid polypeptideHuman islet amyloid polypeptide aggregatesChemistry calculationsAmphiphilic propertiesGeneration spectroscopyΒ-sheetPolypeptide aggregatesIslet amyloid polypeptideΒ-strandsAggregatesAmyloid polypeptideAdsorbAdsorptionSpectroscopyAmyloid proteinInterfacePotential disruptive effects
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