An Anti-Inflammatory PPAR‑γ Agonist from the Jellyfish-Derived Fungus <i>Penicillium chrysogenum</i> J08NF‑4

An investigation of the jellyfish-derived fungus <i>Penicillium chrysogenum</i> J08NF-4 led to the isolation of two new meroterpene derivatives, chrysogenester (<b>1</b>) and 5-farnesyl-2-methyl-1-<i>O</i>-methylhydroquinone (<b>2</b>), and four known farnesyl meroterpenes. Docking analysis of <b>1</b> showed that it binds to PPAR-γ in the same manner as the natural PPAR-γ agonist amorfrutin B (<b>7</b>). Compound <b>1</b> activated PPAR-γ in murine Ac2F liver cells and increased nuclear PPAR-γ protein levels in murine RAW 264.7 macrophages. Because one of the main biological functions of PPAR-γ agonists is to suppress inflammatory response, an <i>in vitro</i> study was performed to explore the anti-inflammatory potency of <b>1</b> and the mechanism involved. In RAW 264.7 macrophages, <b>1</b> inhibited phosphorylation of the NF-κB p65 subunit and suppressed the expression of the pro-inflammatory mediators iNOS, NO, COX-2, TNF-α, IL-1β, and IL-6. We propose <b>1</b> suppresses inflammatory responses by activating PPAR-γ and subsequently downregulating the NF-κB signaling pathway, thus reducing the expressions of pro-inflammatory mediators

Solution Structure of a Sponge-Derived Cystine Knot Peptide and Its Notable Stability

A novel cystine knot peptide, asteropsin E (ASPE), was isolated from an <i>Asteropus</i> sp. marine sponge. The primary, secondary, and tertiary structures of ASPE were determined by high-resolution 2D NMR spectroscopy (900 MHz). With the exception of an <i>N</i>-terminal modification, ASPE shares properties with the previously reported asteropsins A–D, that is, the absence of basic residues, a highly acidic nature, conserved structurally important residues (including two <i>cis</i>-prolines), and a highly conserved tertiary structural framework. ASPE was found to be remarkably stable to gastrointestinal tract enzymes (chymotrypsin, elastase, pepsin, and trypsin) and to human plasma

Dimeric Octaketide Spiroketals from the Jellyfish-Derived Fungus <i>Paecilomyces variotii</i> J08NF‑1

Paeciloketals (<b>1</b>–<b>3</b>), new benzannulated spiroketal derivatives, were isolated from the marine fungus <i>Paecilomyces variotii</i> derived from the giant jellyfish <i>Nemopilema nomurai</i>. Compound <b>1</b> was present as a racemate and was resolved into enantiopure <b>1a</b> and <b>1b</b> by chiral-phase separation on a cellulose column. Compounds <b>2</b> and <b>3</b>, possessing a novel benzannulated spiroketal skeleton, were rapidly interconvertible and yielded an equilibrium mixture on standing at room temperature. The relative and absolute configurations of compounds <b>2</b> and <b>3</b> were determined by NOESY analysis and ECD calculations. Compound <b>1</b> showed modest antibacterial activity against the marine pathogen <i>Vibrio ichthyoenteri</i>

Fumigatosides A–D, Four New Glucosidated Pyrazinoquinazoline Indole Alkaloids from a Jellyfish-Derived Fungus <i>Aspergillus fumigatus</i>

Fumigatosides A–D, Four New Glucosidated Pyrazinoquinazoline Indole Alkaloids from a Jellyfish-Derived Fungus <i>Aspergillus fumigatus</i

PPAR‑γ Agonistic Metabolites from the Ascidian <i>Herdmania momus</i>

Seven new amino acid derivatives (<b>1</b>–<b>4</b> and<b> 6</b>–<b>8</b>) were isolated from MeOH extracts of the marine ascidian <i>Herdmania momus</i>. Planar structures were established on the basis of NMR, IR, and MS spectroscopic analyses. Absolute configurations of these compounds were derived from specific rotation and CD analysis. The peroxisome proliferator-activated receptor (PPAR)-γ agonistic activities of the compounds were investigated due to the similarity of the structural motif to that of the antidiabetic drug rosiglitazone. Analogues with indoleglyoxyl moieties (<b>5</b>, <b>6</b>, and <b>8</b>) showed significant PPAR-γ activation in Ac2F rat liver cells