Redesign of a protein–peptide interaction: Characterization and applications
Jackrel ME, Valverde R, Regan L. Redesign of a protein–peptide interaction: Characterization and applications. Protein Science 2009, 18: 762-774. PMID: 19309728, PMCID: PMC2762588, DOI: 10.1002/pro.75.Peer-Reviewed Original ResearchConceptsProtein-peptide interactionsProtein-peptide pairsPurification applicationsRecognition pairsCorresponding peptide ligandsRepeat protein scaffoldsMolecular recognitionAntibody-antigen interactionsFacile replacementChemical considerationsProtein scaffoldsPeptide ligandsTypical antibody-antigen interactionsHarsh conditionsProtein designModerate affinityScaffoldsPractical applicationsAffinity purificationAffinityLigandsPropertiesInteractionSuccessful applicationDissociationAn AlphaScreen™-Based High-Throughput Screen to Identify Inhibitors of Hsp90-Cochaperone Interaction
Yi F, Zhu P, Southall N, Inglese J, Austin CP, Zheng W, Regan L. An AlphaScreen™-Based High-Throughput Screen to Identify Inhibitors of Hsp90-Cochaperone Interaction. SLAS DISCOVERY 2009, 14: 273-281. PMID: 19211782, PMCID: PMC3066041, DOI: 10.1177/1087057108330114.Peer-Reviewed Original ResearchConceptsImportant anticancer drug targetFirst high-throughput screenHigh-throughput screenChemical probesNovel anticancer drugsAnticancer drug targetSuch moleculesAnticancer drugsTPR2A domainDifferent interactionsCompoundsSmall molecule Hsp90 inhibitorsNovel typeSynthetic peptidesFurther optimizationDrug targetsC-terminal peptideAlphaScreen technologyPeptidesDMSOReported valuesMoleculesInteractionHsp90 inhibitorsBackground ratio