Total Syntheses of Conformationally Constrained Didemnin B Analogues. Replacements of N,O-Dimethyltyrosine with l -1,2,3,4-Tetrahydroisoquinoline and l -1,2,3,4-Tetrahydro-7-methoxyisoquinoline
| Autor: | James E. Tarver, Madeleine M. Joullié, and Amy J. Pfizenmayer |
|---|---|
| Rok vydání: | 2001 |
| Předmět: |
Depsipeptide
Protein Conformation Chemistry Stereochemistry Tetrahydroisoquinoline Organic Chemistry Plasma protein binding Isoquinolines Peptides Cyclic Growth Inhibitors Didemnin B Residue (chemistry) chemistry.chemical_compound Protein structure Depsipeptides Tetrahydroisoquinolines Tumor Cells Cultured Humans Tyrosine Molecule Drug Screening Assays Antitumor Protein Binding |
| Zdroj: | The Journal of Organic Chemistry. 66:7575-7587 |
| ISSN: | 1520-6904 0022-3263 |
| DOI: | 10.1021/jo0105991 |
| Popis: | The design and synthesis of two conformationally constrained analogues of didemnin B are described. The [N,O-Me(2)Tyr(5)]residue of didemnin B was replaced with L-1,2,3,4-tetrahydroisoquinoline-3-carboxylic acid (Tic) and L-1,2,3,4-tetrahydro-7-methoxyisoquinoline-3-carboxylic acid (MeO-Tic), which mimic the N,O-dimethylated tyrosine while constraining the conformation of the molecule. Preliminary results indicate that the conformation of the [N,O-Me(2)Tyr(5)]residue closely matches the conformation imposed by the Tic replacement. |
| Databáze: | OpenAIRE |
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