Tuftelin is expressed in low quantities, and undergoes degradation in the enamel
extracellular matrix. To investigate the structure and function of tuftelin, the full length recombinant human tuftelin protein was produced. The full length human tuftelin cDNA was cloned using Gateway (TM) recombination into the Bac-to-BaC (TM) system compatible transfer vector pDest10. This vector adds a hexahistidine tag to the N-terminus of the expressed protein, enabling one-step affinity purification on nickel column. The recombinant human tuftelin protein was transposed into the bacmid and expressed in Spodoptera frugiperda (SJ9) insect cells. The yield of the purified, his-tagged recombinant full length human Tuftelin (rHTuft(+)) was 5-8 mg/L AZD2281 culture. rHTuft(+) was characterized by SDS-PAGE, Western blot, ESI-TOF spectrometry, restriction mapping and MS/MS sequencing. The availability of the purified, full length recombinant human tuftelin protein opened up the possibility to investigate novel functions of tuftelin. Application of rHTuft(+) agarose beads onto embryonic mouse mandibular selleck chemicals llc explants caused changes in the surrounding epithelial cells, including morphology, orientation and spatial organization. Further studies using
DO labeling, revealed that rHTuft(+), placed on the tooth germ region, brought about recruitment of adjacent embryonic mesenchymal cells. These findings support the hypothesis that tuftelin plays an important role during embryogenesis. (C) 2009 Elsevier Inc. All rights reserved.”
“Aims: Present report describes the in vitro antimalarial activity and docking analysis of seven
4-aminoquinoline-clubbed 1,3,5-triazine derivatives on pf-DHFR-TS.
Methods and Results: The antimalarial activity was evaluated in vitro against chloroquine-sensitive 3D7 strain of Plasmodium falciparum. Compounds were docked onto the active site of pf-DHFR-TS using docking server to explicate necessary structural requirements for antimalarial activity.
Conclusion: RAD001 Title molecules demonstrated considerable bioactivity against the malaria parasite. Docking analysis revealed deep engulfment of the molecules into the inner groove of pf-DHFR-TS active site by making stable ligand-receptor posses. Hydrophobic interaction was identified as the only major interacting force playing a role between ligand-receptor interaction and minor with hydrogen bonds.
Significance and Impact of the study: The study provided the novel insight into the necessary structural requirement for rationale-based antimalarial drug discovery.”
“To investigate neurofilament (NF) dynamics during the cytoskeleton reorganization in regenerating axons, and their electrophysiological and histological consequences, we used two transgenic lines of mice: neurofilament high (NFH)-LacZ and NFH-green fluorescent protein (GFP).