Characterization of Calcium Phosphate Chitosan Nanocomposite as Plant Growth Promoter

In this study, calcium phosphate-chitosan nanocomposite (CaP-CS NC) was prepared by a convenient and affordable co-precipitation method, and the prepared NC was tested for agriculture application.  Physico-chemicals analyses of the CaP-CS NC were conducted by X-ray diffraction (XRD), scanning electron microscope with energy dispersive X-ray spectroscopy (SEM-EDS), Fourier transform infrared spectroscopy (FTIR), and ultraviolet-visible spectroscopy (UV-Vis) instruments to determine the structural characteristics, surface topology, chemical composition, function group, and optical properties. The XRD pattern of CaP-CS NC revealed that the average crystallite size was 43 nm. The SEM images showed agglomeration of the CaP-CS NC with a rod-like shape. The EDS spectrum of the CaP-CS NC indicated the presence of Ca, P, O, and N elements. FTIR displayed vibrational peaks for the active functional group such as carboxylic (C=O), amines (N-H), hydroxyl (O-H), and alkyne (C-H). Furthermore, the spectrum of CaP-CS NC showed the bending mode of phosphates at 588.37 cm-1 and 508.45 cm-1. The UV-Vis-NIR spectrum of the prepared nanocomposite indicates the anti-reflection properties, which might be useful in solar cell applications to increase the efficiency of the solar cell. In addition, the prepared CaP-CS NC was tested for the plant growth stimulator properties at the lab scale level, wherein it exhibited substantial growth. Accordingly, the current study suggests that the prepared CaP-CS NC could be used as a plant growth promoter

Factor quinolinone inhibitors disrupt spindles and multiple LSF (TFCP2)-protein interactions in mitosis, including with microtubule-associated proteins

Factor quinolinone inhibitors (FQIs), a first-in-class set of small molecule inhibitors targeted to the transcription factor LSF (TFCP2), exhibit promising cancer chemotherapeutic properties. FQI1, the initial lead compound identified, unexpectedly induced a concentration-dependent delay in mitotic progression. Here, we show that FQI1 can rapidly and reversibly lead to mitotic arrest, even when added directly to mitotic cells, implying that FQI1-mediated mitotic defects are not transcriptionally based. Furthermore, treatment with FQIs resulted in a striking, concentration-dependent diminishment of spindle microtubules, accompanied by a concentration-dependent increase in multi-aster formation. Aberrant γ-tubulin localization was also observed. These phenotypes suggest that perturbation of spindle microtubules is the primary event leading to the mitotic delays upon FQI1 treatment. Previously, FQIs were shown to specifically inhibit not only LSF DNA-binding activity, which requires LSF oligomerization to tetramers, but also other specific LSF-protein interactions. Other transcription factors participate in mitosis through non-transcriptional means, and we recently reported that LSF directly binds α-tubulin and is present in purified cellular tubulin preparations. Consistent with a microtubule role for LSF, here we show that LSF enhanced the rate of tubulin polymerization in vitro, and FQI1 inhibited such polymerization. To probe whether the FQI1-mediated spindle abnormalities could result from inhibition of mitotic LSF-protein interactions, mass spectrometry was performed using as bait an inducible, tagged form of LSF that is biotinylated by endogenous enzymes. The global proteomics analysis yielded expected associations for a transcription factor, notably with RNA processing machinery, but also to nontranscriptional components. In particular, and consistent with spindle disruption due to FQI treatment, mitotic, FQI1-sensitive interactions were identified between the biotinylated LSF and microtubule-associated proteins that regulate spindle assembly, positioning, and dynamics, as well as centrosome-associated proteins. Probing the mitotic LSF interactome using small molecule inhibitors therefore supported a non-transcriptional role for LSF in mediating progression through mitosis.UL1 TR001430 - NCATS NIH HHS; R01 GM078240 - NIGMS NIH HHSPublished versio