0000000000136277

AUTHOR

Liuqing Yang

showing 5 related works from this author

Synthesis and structure-activity relationship studies of cytotoxic cinnamic alcohol derivatives.

2011

Three series of di- and trisubstituted derivatives of cinnamic alcohol and its conjugated dienol analogues were designed and synthesised. The derivatives were screened for cytotoxicity against nine tumour cell lines: KB, A549, Hela, CNE, PC-3, BEL-7404, HL-60, BGC823 and P388D1. Most of the cinnamic alcohol derivatives showed cytotoxic activity. The compound 7-(4',5'-dichlorobenzyloxy)-6,8-dihydroxycinnamic alcohol (55) exhibited significant cytotoxicity to seven human tumour cell lines on a micromolar range, especially with regard to the KB and P388D1 cell lines, showing IC(50) values of 0.4 and 0.5 µM, respectively. The structure-activity relationships of the derivatives are discussed.

StereochemistryCell SurvivalPropanolsAlcoholAntineoplastic AgentsHL-60 CellsPlant ScienceConjugated systemBiochemistryAnalytical ChemistryHeLachemistry.chemical_compoundStructure-Activity RelationshipCell Line TumorStructure–activity relationshipCytotoxic T cellHumansCytotoxicityCinnamyl alcoholbiologyChemistryOrganic Chemistrybiology.organism_classificationCell cultureDrug Screening Assays AntitumorHeLa CellsNatural product research
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A facile chemoenzymatic approach: one-step syntheses of monoterpenoid indole alkaloids.

2010

Facile chemoenzymatic syntheses of cytotoxic monoterpenoid indole alkaloids with novel skeletons and multiple chiral centers are described. Synthesis of these alkaloids was achieved by a simple one-step reaction using strictosidine and 12-aza-strictosidine as the key intermediates. Strictosidines were prepared by coupling of secologanin with tryptamine and 7-aza-tryptamine, respectively, using the immobilized recombinant Rauvolfia strictosidine synthase. A detailed stereochemical analysis is presented herein. The results provide an opportunity for a chemoenzymatic approach that leads to an increased diversification of complex alkaloids with improved structures and activities.

TryptamineModels MolecularRauvolfiaStrictosidine synthaseStereochemistryOne-StepBiochemistryRauwolfiachemistry.chemical_compoundCarbon-Nitrogen LyasesSecologanin Tryptamine AlkaloidsVinca AlkaloidsAza CompoundsbiologyMolecular StructureOrganic ChemistryGeneral Chemistrybiology.organism_classificationEnzymes ImmobilizedSecologanin Tryptamine AlkaloidsRecombinant ProteinschemistryBiocatalysisStrictosidinebiology.proteinBiocatalysisSecologaninChemistry, an Asian journal
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Improved Expression of His6-Tagged Strictosidine Synthase cDNA for Chemo-Enzymatic Alkaloid Diversification

2010

Strictosidine synthase (STR1) catalyzes the stereoselective formation of 3alpha(S)-strictosidine from tryptamine and secologanin. Strictosidine is the key intermediate in the biosynthesis of 2,000 plant monoterpenoid indole alkaloids, and it is a key precursor of enzyme-mediated synthesis of alkaloids. An improved expression system is described which leads to optimized His(6)-STR1 synthesis in Escherichia coli. Optimal production of STR1 was achieved by determining the impact of co-expression of chaperones pG-Tf2 and pG-LJE8. The amount and activity of STR1 was doubled in the presence of chaperone pG-Tf2 alone. His(6)-STR1 immobilized on Ni-NTA can be used for enzymatic synthesis of stricto…

TryptamineStrictosidine synthaseCatharanthusStereochemistryRecombinant Fusion ProteinsIridoid GlucosidesBioengineeringBiochemistryEnzyme catalysischemistry.chemical_compoundAlkaloidsBiosynthesisCarbon-Nitrogen LyasesHistidineIridoidsVinca AlkaloidsMolecular Biologychemistry.chemical_classificationbiologyGeneral ChemistryGeneral MedicineTryptaminesEnzymechemistryBiochemistryChaperone (protein)StrictosidineBiocatalysisbiology.proteinMolecular MedicineSecologaninOligopeptidesMolecular ChaperonesChemistry & Biodiversity
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Strukturbasis und Enzymmechanismus der Biosynthese von C9- aus C10-monoterpenoiden Indol-Alkaloiden

2009

Alle Neune: Die dreidimensionale Struktur der Polyneuridinaldehyd-Esterase (PNAE) gibt einen Einblick in den Enzymmechanismus der Biosynthese von C9- aus C10-monoterpenoiden Indol-Alkaloiden (siehe Schema). PNAE ist eine sehr substratspezifische Serin-Esterase. Sie enthalt die katalytische Triade S87-D216-H244 und ist ein neues Mitglied der Superfamilie der α/β-Hydrolasen, allerdings mit einer neuartigen Funktion: der Diversifizierung von Alkaloidstrukturen.

General MedicineAngewandte Chemie
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Structural Basis and Enzymatic Mechanism of the Biosynthesis of C9- from C10-Monoterpenoid Indole Alkaloids

2009

Cutting carbons: The three-dimensional structure of polyneuridine aldehyde esterase (PNAE) gives insight into the enzymatic mechanism of the biosynthesis of C(9)- from C(10)-monoterpenoid indole alkaloids (see scheme). PNAE is a very substrate-specific serine esterase. It harbors the catalytic triad S87-D216-H244, and is a new member of the alpha/beta-fold hydrolase superfamily. Its novel function leads to the diversification of alkaloid structures.

Stereochemistrychemistry [Secologanin Tryptamine Alkaloids]polyneuridine aldehyde esterasePolyneuridine-aldehyde esteraseCatalysisSubstrate SpecificityEnzyme catalysischemistry.chemical_compoundProtein structureBiosynthesisHydrolaseCatalytic triadmetabolism [Mutant Proteins]Indole testchemistry.chemical_classificationGeneral ChemistrySecologanin Tryptamine AlkaloidsProtein Structure Tertiarymetabolism [Carboxylic Ester Hydrolases]metabolism [Secologanin Tryptamine Alkaloids]EnzymeAmino Acid SubstitutionchemistryBiochemistryddc:540BiocatalysisMutant ProteinsCarboxylic Ester HydrolasesAngewandte Chemie International Edition
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