Journal: Molecules

Article Title: Design, Synthesis, and Biological Evaluations of a Novel Resveratrol-Type Analogue Against VEGF

doi: 10.3390/molecules30112345

Figure Lengend Snippet: ( A ) Design of resveratrol-type derivatives. ( B ) Synthetic route towards RE-1. (I) 1,3-dichloropropane, NaH, THF, 0 °C-rt, 8 h; (II) pterostilbene, NaH, THF, rt, 16 h, 26%. Docking studies of RES ( C ) and RE-1 ( D ) against VEGF protein. VEGF 1–165 (PDB code: 1FLT) domain was selected as a binding site and docking studies were performed using SEESAR software (13.0 version). RES: resveratrol.

Article Snippet: Prediction of ADMET properties, including TPSA, Log P , intestinal absorption and so on, was conducted under Optibrium mode of SEESAR software (Version 13.0; https://www.biosolveit.de/ , accessed on 11 April 2024). a,b following Lipinski’s Rule of Five.

Techniques: Binding Assay, Software

Journal: Frontiers in Molecular Neuroscience

Article Title: Monoamine Oxidases (MAOs) as Privileged Molecular Targets in Neuroscience: Research Literature Analysis

doi: 10.3389/fnmol.2019.00143

Figure Lengend Snippet: Visualization of the crystal structures of h MAO-A and h MAO-B. The binding mode of irreversible and reversible MAO inhibition on the example of the most prominent MAO-A inhibitor clorgyline (irreversible) and MAO-B inhibitor safinamide (reversible) is represented. (A) Ribbon representation of the co-crystallized structure of clorgyline with the monomer h MAO-A (PDB: 2BXS, resolution: 3.15 Å). The C-terminal membrane region and the N-terminus are depicted. The surface for binding site is colored in gray transparent. (B) Representation of the covalent bonding (1.38 Å) between the irreversible MAO-A inhibitor clorgyline and the FAD co-factor. (C) Ribbon representation of the co-crystallized structure of safinamide with h MAO-B (PDB: 2V5Z, resolution: 1.6 Å). The respective chain A and B of h MAO-B dimer with FAD are depicted. (D) HYDE (HYdrogen bonding and DEsolvation) analysis of desolvation effects and interactions for safinamide (off-white). HYDE visual affinity assessment as embedded in SeeSAR: green = favorable, red = unfavorable and non-colored = no relevant for affinity. The interacting amino acid residues, important water molecules and FAD are shown. Visualization and HYDE analysis were performed using the SeeSAR tool from BioSolveIT (v.8.2, 2019).

Article Snippet: Visualization of the 3D crystal structures of the human MAO-A and human MAO-B enzyme was performed with the SeeSAR software (v.9.0, 2019 form BioSolveIT).

Techniques: Binding Assay, Inhibition, Membrane