Hahk-Soo Kang, Aleksej Krunic, and Jimmy Orjala*
Department of Medicinal Chemistry and Pharmacognosy, University of Illinois at Chicago, 833 S. Wood Street, Chicago, Illinois 60612, United States
J. Nat. Prod., Article ASAP
DOI: 10.1021/np300150h
Publication Date (Web): April 6, 2012
Copyright © 2012 The American Chemical Society and American Society of Pharmacognosy
Stigonemapeptin (
1), a depsipeptide containing an Ahp
(3-amino-6-hydroxy-2-piperidone) residue, was isolated from a bloom
sample of the freshwater cyanobacterium
Stigonema sp. collected
from North Nokomis Lake in the Highland Lake District of northern
Wisconsin. The planar structure was determined by 1D and 2D NMR
experiments as well as HRESIMS analysis. The absolute configurations of
the amino acids were determined using the advanced Marfey’s method after
acid hydrolysis. Stigonemapeptin (
1), characterized by the presence of the Ahp residue, also contained the modified amino acids Abu (2-amino-2-butenoic acid) and
N-formylated Pro. Stigonemapeptin (
1) showed
in vitro elastase and chymotrypsin inhibitory activity, with IC
50 values of 0.26 and 2.93 μM, respectively.
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