Label-free quantitative proteomic analysis of human periodontal ligament stem cells by high-resolution mass spectrometry

2018 ◽  
Vol 54 (1) ◽  
pp. 53-62 ◽  
Author(s):  
Na-Young Han ◽  
Ji-Youn Hong ◽  
Jong-Moon Park ◽  
Changsik Shin ◽  
Saya Lee ◽  
...  
Keyword(s):  
Mass Spectrometry ◽  
Stem Cells ◽  
High Resolution ◽  
Proteomic Analysis ◽  
Periodontal Ligament ◽  
High Resolution Mass Spectrometry ◽  
Label Free ◽  
Periodontal Ligament Stem Cells ◽  
Quantitative Proteomic Analysis ◽  
Resolution Mass

scholarly journals Quantification and Identification of Post-Translational Modifications Using Modern Proteomics

2021 ◽  
pp. 225-235
Author(s):  
Anja Holtz ◽  
Nathan Basisty ◽  
Birgit Schilling
Keyword(s):  
Mass Spectrometry ◽  
High Resolution ◽  
High Throughput ◽  
High Resolution Mass Spectrometry ◽  
Label Free ◽  
Post Translational Modifications ◽  
Data Independent Acquisition ◽  
Lysine Residues ◽  
Detailed Protocol ◽  
Resolution Mass

AbstractPost-translational modifications (PTMs) occur dynamically, allowing cells to quickly respond to changes in the environment. Lysine residues can be targeted by several modifications including acylations (acetylation, succinylation, malonylation, glutarylation, and others), methylation, ubiquitination, and other modifications. One of the most efficient methods for the identification of post-translational modifications is utilizing immunoaffinity enrichment followed by high-resolution mass spectrometry. This workflow can be coupled with comprehensive data-independent acquisition (DIA) mass spectrometry to be a high-throughput, label-free PTM quantification approach. Below we describe a detailed protocol to process tissue by homogenization and proteolytically digest proteins, followed by immunoaffinity enrichment of lysine-acetylated peptides to identify and quantify relative changes of acetylation comparing different conditions.

Exploring the Active Compounds of Traditional Mongolian Medicine Agsirga in Intervention of Novel Coronavirus (2019-nCoV) Based on HPLC-Q-Exactive-MS/MS and Molecular Docking Method

2020 ◽  
Author(s):  
Jie Cheng ◽  
Yuchen Tang ◽  
Baoquan Bao ◽  
Ping Zhang
Keyword(s):  
Mass Spectrometry ◽  
Molecular Docking ◽  
High Resolution ◽  
Mass Spectra ◽  
High Resolution Mass Spectrometry ◽  
Structural Formula ◽  
Active Compounds ◽  
High Resolution Mass ◽  
Q Exactive ◽  
Resolution Mass

<p><a></a><a></a><a></a><a><b>Objective</b></a>: To screen all compounds of Agsirga based on the HPLC-Q-Exactive high-resolution mass spectrometry and find potential inhibitors that can respond to 2019-nCoV from active compounds of Agsirga by molecular docking technology.</p> <p><b>Methods</b>: HPLC-Q-Exactive high-resolution mass spectrometry was adopted to identify the complex components of Mongolian medicine Agsirga, and separated by the high-resolution mass spectrometry Q-Exactive detector. Then the Orbitrap detector was used in tandem high-resolution mass spectrometry, and the related molecular and structural formula were found by using the chemsipider database and related literature, combined with precise molecular formulas (errors ≤ 5 × 10<sup>−6</sup>) , retention time, primary mass spectra, and secondary mass spectra information, The fragmentation regularities of mass spectra of these compounds were deduced. Taking ACE2 as the receptor and deduced compounds as the ligand, all of them were pretreated by discover studio, autodock and Chem3D. The molecular docking between the active ingredients and the target protein was studied by using AutoDock molecular docking software. The interaction between ligand and receptor is applied to provide a choice for screening anti-2019-nCoV drugs.</p> <p><b>Result</b>: Based on the fragmentation patterns of the reference compounds and consulting literature, a total of 96 major alkaloids and stilbenes were screened and identified in Agsirga by the HPLC-Q-Exactive-MS/MS method. Combining with molecular docking, a conclusion was got that there are potential active substances in Mongolian medicine Agsirga which can block the binding of ACE2 and 2019-nCoV at the molecular level.</p>

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