Differential Screening and Mass Mapping of Proteins from Premalignant and Cancer Cell Lines Using Nonporous Reversed-Phase HPLC Coupled with Mass Spectrometric Analysis

2001 ◽  
Vol 73 (6) ◽  
pp. 1219-1227 ◽  
Author(s):  
Bathsheba E. Chong ◽  
Rick L. Hamler ◽  
David M. Lubman ◽  
Stephen P. Ethier ◽  
Allen J. Rosenspire ◽  
...  
Keyword(s):  
Cell Lines ◽  
Cancer Cell ◽  
Cancer Cell Lines ◽  
Reversed Phase ◽  
Mass Spectrometric ◽  
Mass Spectrometric Analysis ◽  
Differential Screening ◽  
Spectrometric Analysis ◽  
Reversed Phase Hplc ◽  
Mass Mapping

scholarly journals New Andrastin-Type Meroterpenoids from the Marine-Derived Fungus Penicillium sp.

Marine Drugs ◽  
2021 ◽  
Vol 19 (4) ◽  
pp. 189
Author(s):  
Jinwei Ren ◽  
Ruiyun Huo ◽  
Gaoran Liu ◽  
Ling Liu
Keyword(s):  
Nuclear Magnetic Resonance ◽  
Magnetic Resonance ◽  
Cell Lines ◽  
Sw480 Cell ◽  
Mass Spectrometric ◽  
Mass Spectrometric Analysis ◽  
Spectrometric Analysis ◽  
Penicillium Species ◽  
Penicillium Sp ◽  
New Compounds

Three new andrastin-type meroterpenoids penimeroterpenoids A–C (1–3) together with two known analogs (4 and 5) were isolated from the cultures of the marine-derived Penicillium species (sp.). The structures of the new compounds were elucidated on the basis of 1- and 2-dimensional (1D/2D) Nuclear Magnetic Resonance (NMR) spectroscopic and mass spectrometric analysis. The absolute configurations of 1–3 were determined by comparison of experimental and calculated electronic circular dichroism (ECD) spectra. Compound 1 showed moderate cytotoxicity against A549, HCT116, and SW480 cell lines.

scholarly journals Pterocarpans from the Root Bark of Aeschynomene Fascicularis

2013 ◽  
Vol 8 (10) ◽  
pp. 1934578X1300801 ◽  
Author(s):  
Edgar Caamal-Fuentes ◽  
Rosa Moo-Puc ◽  
Luis W. Torres-Tapia ◽  
Sergio R. Peraza-Sanchez
Keyword(s):  
Cell Lines ◽  
Cancer Cell ◽  
Cancer Cell Lines ◽  
Mass Spectrometric ◽  
Root Bark ◽  
First Report ◽  
First Time ◽  
Antiproliferative Activities

A new pterocarpan, aeschynocarpin (1), and the known pterocarpan 2-methoxymedicarpin (2) were isolated for the first time from Aeschynomene fascicularis (Fabaceae) and their structures elucidated by means of spectroscopic {UV/Vis, IR, and NMR (1H, 13C, COSY, HMQC, and HMBC)} and mass spectrometric (EI-MS and HRCIMS) techniques. Both compounds were tested in vitro for their cytotoxic and antiproliferative activities against a panel of cancer cell lines. This is the first report on the presence of pterocarpans in the genus Aeschynomene.

scholarly journals Partially Purified Extracts of Sea AnemoneAnemonia viridisAffect the Growth and Viability of Selected Tumour Cell Lines

2016 ◽  
Vol 2016 ◽  
pp. 1-12 ◽  
Author(s):  
Matteo Bulati ◽  
Alessandra Longo ◽  
Tiziana Masullo ◽  
Sara Vlah ◽  
Carmelo Bennici ◽  
...  
Keyword(s):  
Cell Lines ◽  
Cancer Cell ◽  
Human Cancer ◽  
Marine Species ◽  
Cancer Cell Lines ◽  
Reversed Phase ◽  
Cytotoxic Effects ◽  
Human Pbmc ◽  
Human Cancer Cell Lines ◽  
Antiproliferative Activities

In the last few years, marine species have been investigated for the presence of natural products with anticancer activity. Using reversed phase chromatography, low molecular weight proteins were fractionated from the sea anemoneAnemonia viridis. Four different fractions were evaluated for their cytotoxic activity by means of erythrocyte haemolysis test, MTS, and LDH assays. Finally, the antiproliferative activities of three of these fractions were studied on PC3, PLC/PRF/5, and A375 human cancer cell lines. Our analysis revealed that the four fractions showed different protein contents and diverse patterns of activity towards human PBMC and cancer cell lines. Interestingly, fractions III and IV exerted cytotoxic effects on human cells. Conversely, fractions I and II displayed very low toxic effects associated with antiproliferative activities on cancer cell lines.

Targeting the hydrophilic regions of recombinant proteins by MS via in-solution buffer-free trypsin digestion

2019 ◽  
Vol 26 (3) ◽  
pp. 230-237
Author(s):  
Lázaro H Betancourt ◽  
Luis A Espinosa ◽  
Yassel Ramos ◽  
Mónica Bequet-Romero ◽  
Elías N Rodríguez ◽  
...  
Keyword(s):  
Recombinant Proteins ◽  
Posttranslational Modifications ◽  
Reversed Phase ◽  
Glycosylation Site ◽  
Mass Spectrometric ◽  
Mass Spectrometric Analysis ◽  
Mass Spectrometry Analysis ◽  
Core Antigen ◽  
Spectrometric Analysis ◽  
Spectrometry Analysis

A desalting step using reversed phase chromatography is a common practice prior to mass spectrometry analysis of proteolytic digests in spite of the detrimental exclusion of the hydrophilic peptides. The detection of such peptides is also important for the complete coverage of protein sequences and the analysis of posttranslational modifications as inquired by regulatory agencies for the commercialization of biotechnological products. The procedure described here, named in-solution buffer-free digestion, simplifies the sample processing and circumvents the above-mentioned limitations by allowing the detection of tryptic hydrophilic peptides via direct ESI-MS analysis. Two DNA recombinant proteins such as HBcAg (hepatitis B core antigen) and fusion VEGF (vascular endothelial growth factor) were analyzed with the proposed in-solution buffer-free digestion allowing the detection of extremely hydrophilic di-, tri- and tetra-peptides, C-terminal His-tail peptide, as well as disulfide-containing peptides. All these molecular species are hardly seen in mass spectrometric analysis using a standard digestion that includes a C18-desalting step. The procedure was also successfully tried on hydrophilic tetra- and hexa-peptides of Ribonuclease B carrying an N-glycosylation site occupied with “high-mannose” N-glycan chains. The in-solution buffer-free digestion constitutes a simple and straightforward approach to analyse the hydrophilic proteolytic peptides which are commonly elusive to the detection by conventional mass spectrometric analysis.

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