Jizanpeptins, Cyanobacterial Protease Inhibitors from a Symploca sp. Cyanobacterium Collected in the Red Sea

David A. Gallegos; Josep Sauri; Ryan D. Cohen; Xuemei Wan; Patrick Videau; Alec O. Vallota-Eastman; Lamiaa A. Shaala; Diaa T. A. Youssef; R. Thomas Williamson; Gary E. Martin; Benjamin Philmus; Aleksandra E. Sikora; Jane E. Ishmael; Kerry L. McPhail

doi:10.1021/acs.jnatprod.8b00117

Jizanpeptins, Cyanobacterial Protease Inhibitors from a Symploca sp. Cyanobacterium Collected in the Red Sea

David A. Gallegos, Josep Sauri, Ryan D. Cohen, Xuemei Wan, Patrick Videau, Alec O. Vallota-Eastman, Lamiaa A. Shaala, Diaa T. A. Youssef, R. Thomas Williamson, Gary E. Martin, Benjamin Philmus, Aleksandra E. Sikora, Jane E. Ishmael, Kerry L. McPhail

Research output: Indexed journal article › Article › peer-review

20 Citations (Scopus)

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 (IC50 = 72 nM to 1 mu M) compared to chymotrypsin (IC50 = 1.4 to >10 mu M) in vitro and were not overtly cytotoxic to HeLa cervical or NCI-H460 lung cancer cell lines at micromolar concentrations.

Original language	English
Pages (from-to)	1417-1425
Number of pages	9
Journal	Journal of Natural Products
Volume	81
Issue number	6
DOIs	https://doi.org/10.1021/acs.jnatprod.8b00117
Publication status	Published - Jun 2018
Externally published	Yes

Keywords

Marine cyanobacterium
Serine-protease
Vibrio-cholerae
Moorea-producens
High-throughput
Microcystis-aeruginosa
Lyngbya-confervoides
Elastase inhibitors
Cyclic depsipeptide
Fresh-water

UN SDGs

This output contributes to the following UN Sustainable Development Goals (SDGs)

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10.1021/acs.jnatprod.8b00117

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Gallegos, D. A., Sauri, J., Cohen, R. D., Wan, X., Videau, P., Vallota-Eastman, A. O., Shaala, L. A., Youssef, D. T. A., Williamson, R. T., Martin, G. E., Philmus, B., Sikora, A. E., Ishmael, J. E., & McPhail, K. L. (2018). Jizanpeptins, Cyanobacterial Protease Inhibitors from a Symploca sp. Cyanobacterium Collected in the Red Sea. Journal of Natural Products, 81(6), 1417-1425. https://doi.org/10.1021/acs.jnatprod.8b00117

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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 (IC50 = 72 nM to 1 mu M) compared to chymotrypsin (IC50 = 1.4 to >10 mu M) in vitro and were not overtly cytotoxic to HeLa cervical or NCI-H460 lung cancer cell lines at micromolar concentrations.",

keywords = "Marine cyanobacterium, Serine-protease, Vibrio-cholerae, Moorea-producens, High-throughput, Microcystis-aeruginosa, Lyngbya-confervoides, Elastase inhibitors, Cyclic depsipeptide, Fresh-water",

author = "Gallegos, {David A.} and Josep Sauri and Cohen, {Ryan D.} and Xuemei Wan and Patrick Videau and Vallota-Eastman, {Alec O.} and Shaala, {Lamiaa A.} and Youssef, {Diaa T. A.} and Williamson, {R. Thomas} and Martin, {Gary E.} and Benjamin Philmus and Sikora, {Aleksandra E.} and Ishmael, {Jane E.} and McPhail, {Kerry L.}",

year = "2018",

month = jun,

doi = "10.1021/acs.jnatprod.8b00117",

language = "English",

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Gallegos, DA, Sauri, J, Cohen, RD, Wan, X, Videau, P, Vallota-Eastman, AO, Shaala, LA, Youssef, DTA, Williamson, RT, Martin, GE, Philmus, B, Sikora, AE, Ishmael, JE & McPhail, KL 2018, 'Jizanpeptins, Cyanobacterial Protease Inhibitors from a Symploca sp. Cyanobacterium Collected in the Red Sea', Journal of Natural Products, vol. 81, no. 6, pp. 1417-1425. https://doi.org/10.1021/acs.jnatprod.8b00117

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T1 - Jizanpeptins, Cyanobacterial Protease Inhibitors from a Symploca sp. Cyanobacterium Collected in the Red Sea

AU - Gallegos, David A.

AU - Sauri, Josep

AU - Cohen, Ryan D.

AU - Wan, Xuemei

AU - Videau, Patrick

AU - Vallota-Eastman, Alec O.

AU - Shaala, Lamiaa A.

AU - Youssef, Diaa T. A.

AU - Williamson, R. Thomas

AU - Martin, Gary E.

AU - Philmus, Benjamin

AU - Sikora, Aleksandra E.

AU - Ishmael, Jane E.

AU - McPhail, Kerry L.

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N2 - 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 mu M) compared to chymotrypsin (IC50 = 1.4 to >10 mu M) in vitro and were not overtly cytotoxic to HeLa cervical or NCI-H460 lung cancer cell lines at micromolar concentrations.

AB - 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 mu M) compared to chymotrypsin (IC50 = 1.4 to >10 mu M) in vitro and were not overtly cytotoxic to HeLa cervical or NCI-H460 lung cancer cell lines at micromolar concentrations.

KW - Marine cyanobacterium

KW - Serine-protease

KW - Vibrio-cholerae

KW - Moorea-producens

KW - High-throughput

KW - Microcystis-aeruginosa

KW - Lyngbya-confervoides

KW - Elastase inhibitors

KW - Cyclic depsipeptide

KW - Fresh-water

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DO - 10.1021/acs.jnatprod.8b00117

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C2 - 29808677

SN - 0163-3864

VL - 81

SP - 1417

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JO - Journal of Natural Products

JF - Journal of Natural Products

IS - 6

ER -

Jizanpeptins, Cyanobacterial Protease Inhibitors from a Symploca sp. Cyanobacterium Collected in the Red Sea

Abstract

Keywords

UN SDGs

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