1. Jizanpeptins, Cyanobacterial Protease Inhibitors from a Symploca sp. Cyanobacterium Collected in the Red Sea.
- Author
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Gallegos DA, Saurí J, Cohen RD, Wan X, Videau P, Vallota-Eastman AO, Shaala LA, Youssef DTA, Williamson RT, Martin GE, Philmus B, Sikora AE, Ishmael JE, and McPhail KL
- Subjects
- Cell Line, Tumor, Chromatography, High Pressure Liquid methods, Chymotrypsin chemistry, Chymotrypsin pharmacology, Humans, Indian Ocean, Magnetic Resonance Spectroscopy methods, Piperidones chemistry, Piperidones pharmacology, Cyanobacteria chemistry, Depsipeptides chemistry, Depsipeptides pharmacology, Protease Inhibitors chemistry, Protease Inhibitors pharmacology
- Abstract
Jizanpeptins A-E (1-5) are micropeptin depsipeptides isolated from a Red Sea specimen of a Symploca sp. cyanobacterium. The planar structures of the jizanpeptins were established using NMR spectroscopy and mass spectrometry and contain 3-amino-6-hydroxy-2-piperidone (Ahp) as one of eight residues in a typical micropeptin motif, as well as a side chain terminal glyceric acid sulfate moiety. The absolute configurations of the jizanpeptins were assigned using a combination of Marfey's methodology and chiral-phase HPLC analysis of hydrolysis products compared to commercial and synthesized standards. Jizanpeptins A-E showed specific inhibition of the serine protease trypsin (IC
50 = 72 nM to 1 μM) compared to chymotrypsin (IC50 = 1.4 to >10 μM) in vitro and were not overtly cytotoxic to HeLa cervical or NCI-H460 lung cancer cell lines at micromolar concentrations.- Published
- 2018
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