SEDDS Basic Design and Recent Formulation Advancement: A Concurrent Review.

In the present scenario, lipid-based novel drug delivery systems are the area of interest for the formulation scientist in order to improve the bioavailability of poorly water-soluble drugs. A selfemulsifying drug delivery system (SEDDS) upon contact with the gastrointestinal fluid, forms an o/w emulsion. SEDDS has gained popularity as a potential platform for improving the bioavailability of the lipophilic drug by overcoming several challenges. The various advantages like improved solubility, bypassing lymphatic transport, and improvement in bioavailability are associated with SMEDDS or SNEDDS. The extent of the formation of stable SEDDS depends on a specific combination of surfactant, co-surfactant, and oil. The present review highlighted the different aspects of formulation design along with optimization and characterization of SEDDS formulation. It also gives a brief description of the various aspects of the excipients used in SEDDS formulation. This review also includes the conflict between types of SEDDS based on droplet size. There is an extensive review of various research regarding different solidification techniques used for SEDDS in the last three years.

Intranuclear accumulation of plant tubulin in response to low temperature.

Concurrently with cold-induced disintegration of microtubular structures in the cytoplasm, gradual tubulin accumulation was observed in a progressively growing proportion of interphase nuclei in tobacco BY-2 cells. This intranuclear tubulin disappeared upon rewarming. Simultaneously, new microtubules rapidly emerged from the nuclear periphery and reconstituted new cortical arrays, as was shown by immunofluorescence. A rapid exclusion of tubulin from the nucleus during rewarming was also observed in vivo in cells expressing GFP-tubulin. Nuclei were purified from cells that expressed GFP fused to an endoplasmic-reticulum retention signal (BY-2-mGFP5-ER), and green-fluorescent protein was used as a diagnostic marker to confirm that the nuclear fraction was not contaminated by nuclear-envelope proteins. These purified, GFP-free nuclei contained tubulin when isolated from cold-treated cells, whereas control nuclei were void of tubulin. Furthermore, highly conserved putative nuclear-export sequences were identified in tubulin sequences. These results led us to interpret the accumulation of tubulin in interphasic nuclei, as well as its rapid nuclear export, in the context of ancient intranuclear tubulin function during the cell cycle progression.