biostudies-literatureGallegos DAU.S. Department of Health and Human ServicesU.S. Department of CommerceNIGMS NIH HHS1417-1425https://www.ebi.ac.uk/biostudies/studies/S-EPMC7847313biostudies-literatureUnknown81(6)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 (IC₅₀ = 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.Journal of natural productsJizanpeptins, Cyanobacterial Protease Inhibitors from a Symploca sp. Cyanobacterium Collected in the Red Sea.PMC7847313NA10OAR4170064R15 GM122016R15 GM122016-01Shaala LAWilliamson RTYoussef DTAWan XVideau PVallota-Eastman AOCohen RDGallegos DAIshmael JESikora AEMcPhail KLSauri JMartin GEPhilmus BfalseJizanpeptins, Cyanobacterial Protease Inhibitors from a Symploca sp. Cyanobacterium Collected in the Red Sea.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 (IC₅₀ = 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.2018-01-01T00:00:00Z2018 Jun2024-11-06T16:29:49.06Z2021-02-21T05:24:57ZS-EPMC78473132980867710.1021/acs.jnatprod.8b00117