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Depsipeptides from a Guamanian Marine Cyanobacterium, Lyngbya bouillonii, with Selective Inhibition of Serine Proteases.

ABSTRACT: 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 ?M for both) and chymotrypsin (IC(50) = 0.17 and 9.3 ?M, respectively) while showing no inhibition of trypsin (IC(50) > 100 ?M).

SUBMITTER: Rubio BK

PROVIDER: S-EPMC2987581 | biostudies-literature | 2010 Dec

REPOSITORIES: biostudies-literature

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Depsipeptides from a Guamanian Marine Cyanobacterium, Lyngbya bouillonii, with Selective Inhibition of Serine Proteases.

Rubio Brent K BK Parrish Stephen M SM Yoshida Wesley W Schupp Peter J PJ Schils Tom T Williams Philip G PG

Tetrahedron letters 20101201 51

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 μM for both) and chymotrypsin (IC(50) = 0. ...[more]

PMID: 21103388

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