Spectroscopic investigation on shuttlecock-shaped liquid crystalline trimers: Mesomorphic behaviour and its application in optical storage devices.

In this paper, we discuss the synthesis and characterization of 2,3,4-tris[n-((4-(-cyanophenyl)diazenyl)phenoxy)alkyloxy]benzonitrile obtained by coupling 2,3,4-trihydroxy benzonitrile and (E)-4-((4-((n-bromoalkyl)oxy)phenyl)diazenyl)benzonitrile, pertain to shuttlecock shaped liquid crystals. The molecular structure was confirmed by NMR spectroscopic and elemental analyzer. The thermal behavior of the trimers was assessed using a polarizing optical microscope (POM) and differential scanning calorimetry (DSC). The three diazo groups in the trimers enabled us to study the photo-isomerization effect and evaluate their potential applications in optical storage devices. Importantly, we found these trimers easy to synthesize and process, paving the way for cost-effective alternatives to traditional LC materials. We fabricated an optical storage device to study the light effects on shuttlecock-shaped LC trimers, demonstrating that the geometry of the trimers plays a crucial role in determining structure-property relationships.

Novel complex of HAT protein TIP60 and nuclear receptor PXR promotes cell migration and adhesion.

PXR is a member of nuclear receptor superfamily and a well-characterized mediator of xenobiotic metabolism. The classical mode of PXR activation involves its binding to appropriate ligand and subsequent heterodimerization with its partner RXR. However, various factors such as post-translational modifications and crosstalk with different cellular factors may also regulate the functional dynamics and behavior of PXR. In the present study, we have identified that TIP60, an essential lysine acetyltransferase protein interacts with unliganded PXR and together this complex promotes cell migration & adhesion. TIP60 utilizes its NR Box to interact with LBD region of PXR and acetylates PXR at lysine 170 to induce its intranuclear reorganization. Also, RXR is not required for TIP60-PXR complex formation and this complex does not induce ligand-dependent PXR target gene transactivation. Interestingly, we observed that PXR augments the catalytic activity of TIP60 for histones. This is the first report demonstrating the exclusive interaction of TIP60 with PXR and uncovers a potential role for the TIP60-PXR complex in cell migration and adhesion.