2021
DOI: 10.3390/md19080417
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Neuroprotective Effect of Cyclo-(L-Pro-L-Phe) Isolated from the Jellyfish-Derived Fungus Aspergillus flavus

Abstract: Peroxisome proliferator-activated receptor (PPAR) expression has been implicated in pathological states such as cancer, inflammation, diabetes, and neurodegeneration. We isolated natural PPAR agonists—eight 2,5-diketopiperazines—from the jellyfish-derived fungus Aspergillus flavus. Cyclo-(L-Pro-L-Phe) was the most potent PPAR-γ activator among the eight 2,5-DKPs identified. Cyclo-(L-Pro-L-Phe) activated PPAR-γ in Ac2F rat liver cells and SH-SY5Y human neuroblastoma cells. The neuroprotective effect of this par… Show more

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Cited by 4 publications
(7 citation statements)
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“…The binding poses of 1 and amorfrutin 1 were similar to each other, but clearly differed from that of rosiglitazone. The polar moiety of rosiglitazone occupied the region near H11 and H12 by establishing H-bonds with Tyr 473 , His 323 , Ser 289 , and His 449 [ 15 , 19 , 38 ] ( Figure 4 D). The H-bonding with Tyr 473 (essential for H12 conformation) was proposed to be a master keeper for distinguishing the PPAR-γ full agonist from the partial agonist [ 15 , 19 , 38 ].…”
Section: Resultsmentioning
confidence: 99%
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“…The binding poses of 1 and amorfrutin 1 were similar to each other, but clearly differed from that of rosiglitazone. The polar moiety of rosiglitazone occupied the region near H11 and H12 by establishing H-bonds with Tyr 473 , His 323 , Ser 289 , and His 449 [ 15 , 19 , 38 ] ( Figure 4 D). The H-bonding with Tyr 473 (essential for H12 conformation) was proposed to be a master keeper for distinguishing the PPAR-γ full agonist from the partial agonist [ 15 , 19 , 38 ].…”
Section: Resultsmentioning
confidence: 99%
“…The polar moiety of rosiglitazone occupied the region near H11 and H12 by establishing H-bonds with Tyr 473 , His 323 , Ser 289 , and His 449 [ 15 , 19 , 38 ] ( Figure 4 D). The H-bonding with Tyr 473 (essential for H12 conformation) was proposed to be a master keeper for distinguishing the PPAR-γ full agonist from the partial agonist [ 15 , 19 , 38 ]. However, partial agonists mainly occupy the region between H3 and β-sheet, and stabilize the conformation of the LBD through an H-bond with Ser 342 (β-sheet) and hydrophobic interactions with H3 [ 15 , 19 ].…”
Section: Resultsmentioning
confidence: 99%
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