1.Synthesis of (2β,3α,6-(2)H3)cholesteryl linoleate and cholesteryl oleate as internal standards for mass spectrometry.
Miura Y1, Hui SP2, Shrestha R1, Hiruma T1, Takeda S1, Fuda H1, Ikegawa S1, Hirano K3, Chiba H1. Steroids. 2016 Mar;107:1-9. doi: 10.1016/j.steroids.2015.12.004. Epub 2015 Dec 17.
The accurate analysis of trace component in complex biological matrices requires the use of reliable standards. For liquid chromatography/mass spectrometry analysis, the stable isotope-labeled derivatives of the analyte molecules are the most appropriate internal standards. We report here the synthesis of (2β,3α,6-(2)H3)cholesteryl linoleate and oleate containing three non-exchangeable deuterium in the steroid ring. The principal reactions used were: (1) trans diaxial opening of 2α,3α-epoxy-6-oxo-5α-cholestane with LiAlD4 and subsequent oxidation of the resulting (2β,6α-(2)H2)-3α,6β-diol with Jones' reagent, followed by reduction of the resulting (2β-(2)H)-3,6-dione with NaBD4 leading to the (2β,3α,6α-(2)H3)-3β,6β-dihydroxy-5α-cholestane, (2) selective protection of the 3β-hydroxy group as the tert-butyldimethylsilyl ether, (3) dehydration of the 6β-hydroxy group with POCl3 and removal of tert-butyldimethylsilyloxy groups with 5M HCl in acetone, and (4) esterification of the resultant (2β,3α,6-(2)H3)cholesterol with linoleic and oleic acids using 1-(3-dimethylaminopropyl)-3-ethylcarbodiimide.
2.Surface decorated nanoparticles as surrogate carriers for improved transport and absorption of epirubicin across the gastrointestinal tract: Pharmacokinetic and pharmacodynamic investigations.
Tariq M1, Alam MA2, Singh AT3, Panda AK4, Talegaonkar S5. Int J Pharm. 2016 Mar 30;501(1-2):18-31. doi: 10.1016/j.ijpharm.2016.01.054. Epub 2016 Jan 23.
Epirubicin (EPI) is a P-gp substrate antracycline analogue which elicits poor oral bioavailability. In the present work, EPI loaded poly-lactide-co-glycolic acid nanoparticles (PLGA-NPs) were prepared by double emulsion approach and superficially decorated with polyethylene glycol (EPI-PNPs) and mannosamine (EPI-MNPs). Average hydrodynamic particle size of EPI-PNPs and EPI-MNPs was found 248.63±12.36 and 254.23±15.16nm, respectively. Cytotoxicity studies were performed against human breast adenocarcinoma cell lines (MCF-7) confirmed the superiority of EPI-PNPs and EPI-MNPs over free epirubicin solution (EPI-S). Further, confocal laser scanning microscopy (CLSM) and flow cytometric analysis (FACS) demonstrated enhanced drug uptake through EPI-PNPs and EPI-MNPs and elucidated dominance of caveolae mediated endocytosis for NPs uptake. Cellular transport conducted on human colon adenocarcinoma cell line (Caco-2) showed 2.45 and 3.17 folds higher permeability of EPI through EPI-PNPs and EPI-MNPs when compared with EPI-S (p<0.
3.Novel hybrid structure silica/CdTe/molecularly imprinted polymer: synthesis, specific recognition, and quantitative fluorescence detection of bovine hemoglobin.
Li DY1, He XW, Chen Y, Li WY, Zhang YK. ACS Appl Mater Interfaces. 2013 Dec 11;5(23):12609-16. doi: 10.1021/am403942y. Epub 2013 Nov 25.
This work presented a novel strategy for the synthesis of the hybrid structure silica/CdTe/molecularly imprinted polymer (Si-NP/CdTe/MIP) to recognize and detect the template bovine hemoglobin (BHb). First, amino-functionalized silica nanoparticles (Si-NP) and carboxyl-terminated CdTe quantum dots (QDs) were assembled into composite nanoparticles (Si-NP/CdTe) using the EDC (1-(3-dimethylaminopropyl)-3-ethylcarbodiimide hydrochloride) chemistry. Next, Si-NP/CdTe/MIP was synthesized by anchoring molecularly imprinted polymer (MIP) layer on the surface of Si-NP/CdTe through the sol-gel technique and surface imprinting technique. The hybrid structure possessed the selectivity of molecular imprinting technique and the sensitivity of CdTe QDs as well as well-defined morphology. The binding experiment and fluorescence method demonstrated its special recognition performance toward the template BHb. Under the optimized conditions, the fluorescence intensity of the Si-NP/CdTe/MIP decreased linearly with the increase of BHb in the concentration range 0.
4.Site-directed immobilization of antibody using EDC-NHS-activated protein A on a bimetallic-based surface plasmon resonance chip.
Sohn YS, Lee YK. J Biomed Opt. 2014 May;19(5):051209. doi: 10.1117/1.JBO.19.5.051209.
The characteristics of a waveguide-coupled bimetallic surface plasmon resonance (WcBiM SPR) sensor using (3-dimethylaminopropyl)-3-ethylcarbodiimide(EDC)-N-hydroxysuccinimide(NHS)-activated protein A was investigated, and the detection of IgG using the EDC-NHS-activated protein A was studied in comparison with protein A and a self-assembled monolayer (SAM). The WcBiM sensor, which has a narrower full width at half maximum (FWHM) and a steeper slope, was selected since it leads to a larger change in the reflectance in the intensity detection mode. A preparation of the EDC-NHS-activated protein A for site-directed immobilization of antibodies was relative easily compared to the engineered protein G and A. In antigen-antibody interactions, the response to IgG at the concentrations of 50, 100, and 150 ng/ml was investigated. The results showed that the sensitivity of the WcBiM sensor using the EDC-NHS-activated protein A, protein A, and SAM was 0.
