Comprehensive characterization of the in vitro and in vivo metabolites of limonin in human samples using LC-Q-TOF/MS

2017 ◽  
Vol 1068-1069 ◽  
pp. 226-232 ◽  
Author(s):  
Shijia Liu ◽  
Peidong Chen ◽  
Nongshan Zhang ◽  
Luning Sun ◽  
Guoliang Dai ◽  
...  
RSC Advances ◽  
2020 ◽  
Vol 10 (18) ◽  
pp. 10431-10446
Author(s):  
Wenjing Sun ◽  
Yiran Jin ◽  
Shuai Guan ◽  
Mengxin Yang ◽  
Miaoting Zhang ◽  
...  

The experimental process flow.


Antioxidants ◽  
2021 ◽  
Vol 10 (3) ◽  
pp. 427
Author(s):  
Priya Muralidharan ◽  
Maria F. Acosta ◽  
Alexan I. Gomez ◽  
Carissa Grijalva ◽  
Haiyang Tang ◽  
...  

This is the first study reporting on the design and development innovative inhaled formulations of the novel natural product antioxidant therapeutic, tetramethylpyrazine (TMP), also known as ligustrazine. TMP is obtained from Chinese herbs belonging to the class of Ligusticum. It is known to have antioxidant properties. It can act as a Nrf2/ARE activator and a Rho/ROCK inhibitor. The present study reports for the first time on the comprehensive characterization of raw TMP (non-spray dried) and spray dried TMP in a systematic manner using thermal analysis, electron microscopy, optical microscopy, and Raman spectroscopy. The in vitro aerosol dispersion performance of spray dried TMP was tested using three different FDA-approved unit-dose capsule-based human dry powder inhaler devices. In vitro human cellular studies were conducted on pulmonary cells from different regions of the human lung to examine the biocompatibility and non-cytotoxicity of TMP. Furthermore, the efficacy of inhaled TMP as both liquid and dry powder inhalation aerosols was tested in vivo using the monocrotaline (MCT)-induced PH rat model.


2016 ◽  
Vol 79 (21-22) ◽  
pp. 1479-1490 ◽  
Author(s):  
Xiaobin Li ◽  
Minghai Tang ◽  
Hairong Wang ◽  
Liang Ma ◽  
Haoyu Ye ◽  
...  

2019 ◽  
Author(s):  
Priya Prakash ◽  
Travis Lantz ◽  
Krupal P. Jethava ◽  
Gaurav Chopra

Amyloid plaques found in the brains of Alzheimer’s disease (AD) patients primarily consists of amyloid beta 1-42 (Ab42). Commercially, Ab42 is synthetized using peptide synthesizers. We describe a robust methodology for expression of recombinant human Ab(M1-42) in Rosetta(DE3)pLysS and BL21(DE3)pLysS competent E. coli with refined and rapid analytical purification techniques. The peptide is isolated and purified from the transformed cells using an optimized set-up for reverse-phase HPLC protocol, using commonly available C18 columns, yielding high amounts of peptide (~15-20 mg per 1 L culture) in a short time. The recombinant Ab(M1-42) forms characteristic aggregates similar to synthetic Ab42 aggregates as verified by western blots and atomic force microscopy to warrant future biological use. Our rapid, refined, and robust technique to purify human Ab(M1-42) can be used to synthesize chemical probes for several downstream in vitro and in vivo assays to facilitate AD research.


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