期刊
AMINO ACIDS
卷 38, 期 3, 页码 691-700出版社
SPRINGER WIEN
DOI: 10.1007/s00726-009-0267-2
关键词
Ornithine; Sulfamoyl group; Arginine bioisosteres; Tripeptides; Thrombin inhibitors; Anticoagulants
资金
- Ministero dell'Universita e della Ricerca (MIUR, Italy)
Sulfamoylation of the l-ornithine methyl ester side-chain generates a non-natural arginine isostere which can be coupled with N-Fmoc-l-proline to synthesize analogues which maintain the structural characteristics of the biologically important Pro-Arg dipeptide sequence. As a probe of its biological importance, the sulfamoylated amino acid derivative was also incorporated as P1 residue in tripeptide structures matching the C-terminal subsequence of fibrinogen. The reported results demonstrate that the functionalization of l-ornithine side-chain with a neutral sulfamoyl group can generate an arginine bioisostere which can be used for the synthesis of prototypes of a new class of human thrombin inhibitors.
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