MOESM1 of Histone isoform H2A1H promotes attainment of distinct physiological states by altering chromatin dynamics

Additional file 1: Figure S1. Multiple alignment of all the H2A protein sequences in rat. Figure S2. RP-HPLC chromatogram of histones isolated from the rat liver tissue. Figure S3. Unique peptides identified for the H2A isoforms. Figure S4. Real-time PCR of H2A isoforms in the normal vs tumor liver tissues. Figure S5. H2A.1 and H2A.2 isoforms in the CL44 and CL38 cells. Figure S6. Migration and cell proliferation upon overexpression of the histone H2A isoforms. Figure S7. Sequence comparison of H2A isoforms. Figure S8. Approach for equilibrium unfolding analysis of histone dimers. Figure S9. Guanidine chloride induced denaturation of H2A-H2B dimer. Figure S10. RMSD of MDS. Figure S11. Primers

Acetylcholinesterase and Aβ Aggregation Inhibition by Heterometallic Ruthenium(II)–Platinum(II) Polypyridyl Complexes

Two heteronuclear ruthenium­(II)–platinum­(II) complexes [Ru­(bpy)₂(BPIMBp)­PtCl₂]²⁺ (<b>3</b>) and [Ru­(phen)₂(BPIMBp)­PtCl₂]²⁺ (<b>4</b>), where bpy = 2,2′-bipyridine, phen = 1,10-phenanthroline, and BPIMBp = 1,4′-bis­[(2-pyridin-2-yl)-1H-imidazol-1-ylmethyl]-1,1′-biphenyl, have been designed and synthesized from their mononuclear precursors [Ru­(bpy)₂(BPIMBp)]²⁺ (<b>1)</b> and [Ru­(phen)₂(BPIMBp)]²⁺ (<b>2</b>) as multitarget molecules for Alzheimer’s disease (AD). The inclusion of the cis-PtCl₂ moiety facilitates the covalent interaction of Ru­(II) polypyridyl complexes with amyloid β (Aβ) peptide. These multifunctional complexes act as inhibitors of acetylcholinesterase (AChE), Aβ aggregation, and Cu-induced oxidative stress and protect neuronal cells against Aβ-toxicity. The study highlights the design of metal based anti-Alzheimer’s disease (AD) systems