537-49-5Relevant articles and documents
PF1163A and B, new antifungal antibiotics produced by Penicilium sp. II. Physico-chemical properties and structure elucidation
Sasaki, Toru,Nose, Hiroshi,Hosoya, Ayako,Yoshida, Shigemi,Kawaguchi, Mami,Watanabe, Takashi,Usui, Takayuki,Ohtsuka, Yasuo,Shomura, Takashi,Takano, Satoko,Tatsuta, Kuniaki
, p. 38 - 44 (2000)
The structures of new antifungal antibiotics, PF1163A and B, were elucidated by spectroscopic analyses of the degradation products and by X-ray crystallography of the de-2-hydroxyethyl derivative of PF1163B. Both antibiotics consist:of a 13-membered macrocyclic structure containing a derivative of N-methyl tyrosine and a hydroxy fatty acid. PF1163A differs from PF1163B by having an additional hydroxyl group on the side chain.
Structural Diversity and Anticancer Activity of Marine-Derived Elastase Inhibitors: Key Features and Mechanisms Mediating the Antimetastatic Effects in Invasive Breast Cancer
Al-Awadhi, Fatma H.,Paul, Valerie J.,Luesch, Hendrik
, p. 815 - 825 (2018/03/27)
Three new 3-amino-6-hydroxy-2-piperidone (Ahp)-containing cyclic depsipeptides, named loggerpeptins A–C (1–3), along with molassamide (4), were discovered from a marine cyanobacterium, extending the structural diversity of this prevalent scaffold of cyanobacterial serine protease inhibitors. Molassamide, which contains a 2-amino-butenoic (Abu) unit in the cyclic core, was the most potent and selective analogue against human neutrophil elastase (HNE). Given the growing evidence supporting the role of HNE in breast cancer progression and metastasis, we assessed the cellular effects of compounds 3 and 4 in the context of targeting invasive breast cancer. Both compounds inhibited cleavage of the elastase substrate CD40 in biochemical assays; however, only 4 exhibited significant cellular activity. As CD40 and other receptor proteolytic processing culminates in NFκB activation, we assessed the effects of 4 on the expression of target genes, including ICAM-1. ICAM-1 is also a direct target of elastase and, in our studies, compound 4 attenuated both elastase-induced ICAM-1 gene expression and ICAM-1 proteolytic processing by elastase, revealing a potential dual effect on migration through modulation of gene expression and proteolytic processing. Molassamide also specifically inhibited the elastase-mediated migration of highly invasive triple-negative breast cancer cells.
Kurahamide, a cyclic depsipeptide analog of dolastatin 13 from a marine cyanobacterial assemblage of Lyngbya sp.
Iwasaki, Arihiro,Sumimoto, Shinpei,Ohno, Osamu,Suda, Shoichiro,Suenaga, Kiyotake
, p. 609 - 613 (2014/06/09)
Kurahamide, a new dolastatin 13 analog, was isolated from a marine cyanobacterial assemblage, consisting mostly of Lyngbya sp. Its gross structure was elucidated by spectroscopic analysis, and the stereochemistries were assigned based on a chiral HPLC analysis of hydrolysis products. Kurahamide strongly inhibited elastase and chymotrypsin in vitro. In addition, kurahamide moderately inhibited the growth of human cancer cells, including HeLa and HL60 cells.
Stigonemapeptin, an Ahp-containing depsipeptide with elastase inhibitory activity from the bloom-forming freshwater cyanobacterium Stigonema sp.
Kang, Hahk-Soo,Krunic, Aleksej,Orjala, Jimmy
experimental part, p. 807 - 811 (2012/06/29)
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 IC50 values of 0.26 and 2.93 μM, respectively.