Journal: bioRxiv

Article Title: A small molecule PTER-selective inhibitor reduces food intake and body weight

doi: 10.64898/2026.01.26.701829

Figure Lengend Snippet: (A) Superposition of human HDAC(1-11) structures showing conserved aromatic side chains in active site. Average distance between two side chain is labeled. PDB IDs are 4BKX, 4LXZ, 4A69, 2VQJ, 5EDU, 3C0Y, 1T64 for human HDAC 1-4, 6-8. HDAC5 and 9-11 are AlphaFold-predicted models. The representative SAHA (white) is from an HDAC2 co-crystal structure (PDB ID 4LXZ). (B) Superposition of the top poses of docked PTERi (yellow) in sPTER and docked SAHA in sPTER, and SAHA from an HDAC2 co-crystal structure (PDB ID 4LXZ). Superposition is based on the top-ranked SAHA pose in sPTER and SAHA pose in HDAC2. SAHA poses are not shown for simplicity. Side chains of sPTER are shown in purple, while side chains of HDAC2 are shown in white. (C) Chemical structure of PTERi. (D) Dose-response inhibition of PTER activity by PTERi. (E) Heat map of dose-response inhibition for PTERi against the indicated recombinant enzyme. (F, G) Lineweaver-Burke plot (F) and dose-response inhibition of PTERi (G) in PTER activity assays. For (D-G) , PTER activity (N-acetyltaurine hydrolysis) was measured by quantifying taurine production using 200 ng of purified recombinant mouse PTER (mPTER, panels D-G ) or purified recombinant PTER from the indicated species (G) and 100 µM N-acetyltaurine for 1 h at 37°C. N=3/data point for (D,G) and N=1/data point for (E,F) . (D,G) are shown as mean ± SEM. IC 50 values for were determined from the dose-response curves via nonlinear regression analysis using GraphPad Prism.

Article Snippet: The HDAC assay was performed in 50 μl reaction volume containing the HDAC reaction assay buffer, 600 μg of the liver lysate, 100 μM HDAC substrate peptide Ac-Arg-Gly-Lys-Ac-Glu-AMC (custom synthesized by Elim Biopharm), and 10 μM of indicated inhibitors.

Techniques: Labeling, Inhibition, Activity Assay, Recombinant, Purification

Journal: Molecules

Article Title: Identification, Molecular Docking Mechanism and Cellular Activity of Selenium-Enriched ACE Inhibitory Peptides from Oysters

doi: 10.3390/molecules30244818

Figure Lengend Snippet: ACE inhibitory activities for Se-enriched oyster hydrolysates prepared by different proteases. Bars with different lowercase letters indicate significant differences ( p < 0.05) as determined by Tukey’s test.

Article Snippet: Two novel Se-enriched oyster-derived ACE inhibitory peptides were artificially synthesized by Synpeptide Co., Ltd. (Nanjing, China).

Techniques:

Journal: Molecules

Article Title: Identification, Molecular Docking Mechanism and Cellular Activity of Selenium-Enriched ACE Inhibitory Peptides from Oysters

doi: 10.3390/molecules30244818

Figure Lengend Snippet: ( A ) Chromatogram profiles for the ultrafiltration fraction (MW < 10 kDa) of Se-enriched oyster hydrolysate acquired by preparative RP-HPLC at the absorption wavelengths of 214 nm (pink curve) and 280 nm (black curve); ( B ) the ACE inhibitory activity for the fractions of M1, M2, M3, M4 and M5 estimated at 1.0 mg/mL; ( C ) chromatogram profiles for the M4 fraction by preparative RP-HPLC; ( D ) the ACE inhibitory activity for the fractions of M4-1, M4-2 and M4-3 measured at 1.0 mg/mL.

Article Snippet: Two novel Se-enriched oyster-derived ACE inhibitory peptides were artificially synthesized by Synpeptide Co., Ltd. (Nanjing, China).

Techniques: Activity Assay

Journal: Molecules

Article Title: Identification, Molecular Docking Mechanism and Cellular Activity of Selenium-Enriched ACE Inhibitory Peptides from Oysters

doi: 10.3390/molecules30244818

Figure Lengend Snippet: Effect of oyster-derived Se-enriched ACE inhibitory peptides on the cell viability of EA.hy926 cells.

Article Snippet: Two novel Se-enriched oyster-derived ACE inhibitory peptides were artificially synthesized by Synpeptide Co., Ltd. (Nanjing, China).

Techniques: Derivative Assay

Journal: Molecules

Article Title: Identification, Molecular Docking Mechanism and Cellular Activity of Selenium-Enriched ACE Inhibitory Peptides from Oysters

doi: 10.3390/molecules30244818

Figure Lengend Snippet: Effect of Se-enriched oyster-derived ACE inhibitory peptides on the NO production ( A ) and the ET-1 secretion ( B ) of EA.hy 926 cells. Different letters in the same test indicate significant differences ( p < 0.05).

Article Snippet: Two novel Se-enriched oyster-derived ACE inhibitory peptides were artificially synthesized by Synpeptide Co., Ltd. (Nanjing, China).

Techniques: Derivative Assay