Prenylation at the indole ring leads to a significant increase of cytotoxicity of tryptophan-containing cyclic dipeptides

Bioorganic and Medicinal Chemistry Letters

Volumn 22, Issue 12, 2012, Pages 3866-3869

  Wollinsky, Beate ^a   Ludwig, Lena ^a   Hamacher, Alexandra ^b   Yu, Xia ^a   Kassack, Matthias U ^b   Li, Shu Ming ^a  

^a PHILIPPS UNIVERSITY MARBURG   (Germany)

^b HEINRICH HEINE UNIVERSITY   (Germany)

Author keywords

Chemoenzymatic synthesis; Cyclic dipeptides; Cytotoxicity; Prenylated derivatives; Prenyltransferase

Indexed keywords

ALANINE; DIMETHYLALLYL DIPHOSPHATE; DIPEPTIDE; FTMPT1 PROTEIN; INDOLE DERIVATIVE; PROLINE; RECOMBINANT PROTEIN; TRYPTOPHAN; TRYPTOPHAN CONTAINING CYCLIC DIPEPTIDE; UNCLASSIFIED DRUG;

AMINO ACID SEQUENCE; ANIMAL CELL; ARTICLE; CANCER CELL CULTURE; CATALYST; CONTROLLED STUDY; DRUG CYTOTOXICITY; ENZYME ISOLATION; ENZYME STRUCTURE; ENZYME SYNTHESIS; FEMALE; HIGH PERFORMANCE LIQUID CHROMATOGRAPHY; HUMAN; HUMAN CELL; LEUKEMIA CELL; LEUKEMIA CELL LINE; MASS SPECTROMETRY; NONHUMAN; OVARY CANCER; PRENYLATION; RING OPENING; STEREOCHEMISTRY; STEREOISOMERISM;

ALANINE; BIOCATALYSIS; CELL LINE, TUMOR; CELL SURVIVAL; CHROMATOGRAPHY, HIGH PRESSURE LIQUID; DIMETHYLALLYLTRANSTRANSFERASE; DIPEPTIDES; FUNGAL PROTEINS; HEMITERPENES; HUMANS; INDOLES; INHIBITORY CONCENTRATION 50; MAGNETIC RESONANCE SPECTROSCOPY; ORGANOPHOSPHORUS COMPOUNDS; PEPTIDES, CYCLIC; PRENYLATION; PROLINE; RECOMBINANT PROTEINS; STEREOISOMERISM; STRUCTURE-ACTIVITY RELATIONSHIP; SUBSTRATE SPECIFICITY; TRYPTOPHAN;

EID: 84861576805     PISSN: 0960894X     EISSN: 14643405     Source Type: Journal    
DOI: 10.1016/j.bmcl.2012.04.119     Document Type: Article

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