Depsipeptides from a Guamanian marine cyanobacterium, Lyngbya bouillonii, with selective inhibition of serine proteases

✍ Scribed by Brent K. Rubio; Stephen M. Parrish; Wesley Yoshida; Peter J. Schupp; Tom Schils; Philip G. Williams

• Book ID: 104098468
• Publisher: Elsevier Science
• Year: 2010
• Tongue: French
• Weight: 247 KB
• Volume: 51
• Category: Article
• ISSN: 0040-4039
• DOI: 10.1016/j.tetlet.2010.10.062

✦ Synopsis

Bouillomides A (1) and B (2) are two depsipeptide analogues of dolastatin 13. Isolated from a Guamanian sample of Lyngbya bouillonii, the planar structures were elucidated on the basis of HR-ESI-MS and NMR data, while the absolute configurations were determined by employing functional group conversions, modified Marfey's analysis, and detailed analyses of ROESY correlations. Compounds 1 and 2 selectively inhibited serine proteases elastase (IC 50 = 1.9 lM for both) and chymotrypsin (IC 50 = 0.17 and 9.3 lM, respectively) while showing no inhibition of trypsin (IC 50 >100 lM).