Journal
AMINO ACIDS
Volume 38, Issue 3, Pages 691-700Publisher
SPRINGER WIEN
DOI: 10.1007/s00726-009-0267-2
Keywords
Ornithine; Sulfamoyl group; Arginine bioisosteres; Tripeptides; Thrombin inhibitors; Anticoagulants
Categories
Funding
- Ministero dell'Universita e della Ricerca (MIUR, Italy)
Ask authors/readers for more resources
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.
Authors
I am an author on this paper
Click your name to claim this paper and add it to your profile.
Reviews
Recommended
No Data Available