A novel nanomicelle composed from PEGylated TB di-peptide could be successfully used as a BCG booster.

Objectives: Tuberculosis affects one-third of the world's population and leads to a high rate of morbidity and mortality. Bacillus Chalmette-Guerin (BCG) as the only approved vaccine for the Mycobacterium tuberculosis (Mtb) does not show enough protection in the vaccinated population. Materials and Methods: The main aim of this study was to prepare a self-assembled nanomicelle composed from a di-block polymer in which, a di-fusion peptide was the hydrophobic block and polyethylene glycol (PEG) was the hydrophilic block. The micelles were characterized in vitro and in vivo as an antigen delivery system/adjuvant both with and without a prime BCG. Results: The micellar nanovaccine was able to elicit good dendritic cell maturation. Nanomicelles could efficiently induce systemic cytokines as well as nasal secretory predominant antibody titers (sIgA). The expression pattern of cytokines indicated the superiority of cellular immunity. Nasal administration of two doses of nanomicelles after a prime subcutaneous administration of BCG induced the highest mucosal and systemic immune responses. Conclusion: Based on our results PEG-HspX/EsxS self-assembled nanomicelle is highly immunogenic and can be considered a potential vaccine candidate against Mtb to boost BCG efficiency.

Proteomics screening of molecular targets of curcumin in mouse brain.

AIMS: Curcumin is one of the most important constituent of Curcuma longa L. with antioxidant, anti-inflammatory and anticancer effects. In this study, we investigated potential intracellular targets of curcumin by affinity chromatography based on target deconvolution. Identification of curcumin interacting proteins may help in evaluating biological and side effects of this natural compound. MAIN METHODS: Curcumin was immobilized through a linker to sepharose beads as solid matrix. Pull down assay was performed by passing tissue lysate of mouse brain through the column to enrich and purify curcumin interacting proteins. Then proteins were separated using two-dimensional gel electrophoresis and identified using MALDI/TOF/TOF mass spectrometry. KEY FINDINGS: Our results show that curcumin physically binds to a wide range of cellular proteins including structural proteins, metabolic enzymes and proteins involved in apoptosis pathway. SIGNIFICANCE: Finding curcumin interacting proteins may help in understanding a part of curcumin pharmacological effects.