Identification and discrimination of binding sites of an organoruthenium anticancer complex to single-stranded oligonucleotides by mass spectrometry

The Analyst ◽  
2014 ◽  
Vol 139 (18) ◽  
pp. 4491-4496 ◽  
Author(s):  
Suyan Liu ◽  
Kui Wu ◽  
Wei Zheng ◽  
Yao Zhao ◽  
Qun Luo ◽  
...  
Keyword(s):  
Mass Spectrometry ◽  
Binding Sites ◽  
Top Down ◽  
Ms Analysis ◽  
Ladder Sequencing ◽  
Bulky Ligand

Top-down MS analysis provided sequential and complementary fragments, which is more efficient than ladder-sequencing MS in discriminating binding sites of a ruthenium anticancer complex bearing a bulky ligand to oligonucleotides.

scholarly journals Probing ligand and cation binding sites in G-quadruplex nucleic acids by mass spectrometry and electron photodetachment dissociation sequencing

The Analyst ◽  
2019 ◽  
Vol 144 (11) ◽  
pp. 3518-3524 ◽  
Author(s):  
Dababrata Paul ◽  
Adrien Marchand ◽  
Daniela Verga ◽  
Marie-Paule Teulade-Fichou ◽  
Sophie Bombard ◽  
...  
Keyword(s):  
Mass Spectrometry ◽  
Tandem Mass Spectrometry ◽  
Ligand Binding ◽  
Binding Sites ◽  
Cation Binding ◽  
Tandem Mass ◽  
Top Down ◽  
G Quadruplex ◽  
Ligand Binding Sites ◽  
Electron Photodetachment

Tandem mass spectrometry: native top-down sequencing by electron photodetachment dissociation (EPD) reveals ligand binding sites on DNA G-quadruplexes.

Top-Down ESI-ECD-FT-ICR Mass Spectrometry Localizes Noncovalent Protein-Ligand Binding Sites

2006 ◽  
Vol 128 (45) ◽  
pp. 14432-14433 ◽  
Author(s):  
Yongming Xie ◽  
Jennifer Zhang ◽  
Sheng Yin ◽  
Joseph A. Loo
Keyword(s):  
Mass Spectrometry ◽  
Ligand Binding ◽  
Binding Sites ◽  
Top Down ◽  
Ligand Binding Sites ◽  
Noncovalent Protein ◽  
Ft Icr

Covalent-Fragment Screening of Brd4 Identifies a Ligandable Site Orthogonal to the Acetyl-Lysine Binding Sites

2019 ◽  
Author(s):  
Michael Olp ◽  
Daniel Sprague ◽  
Stefan Kathman ◽  
Ziyang Xu ◽  
Alexandar Statsyuk ◽  
...  
Keyword(s):  
Mass Spectrometry ◽  
Binding Site ◽  
Binding Sites ◽  
Computational Prediction ◽  
Chemical Probes ◽  
Computational Docking ◽  
Fragment Screening ◽  
Covalent Inhibitors ◽  
Bet Protein ◽  
Proof Of Principle

<p>Brd4, a member of the bromodomain and extraterminal domain (BET) family, has emerged as a promising epigenetic target in cancer and inflammatory disorders. All reported BET family ligands bind within the bromodomain acetyl-lysine binding sites and competitively inhibit BET protein interaction with acetylated chromatin. Alternative chemical probes that act orthogonally to the highly-conserved acetyl-lysine binding sites may exhibit selectivity within the BET family and avoid recently reported toxicity in clinical trials of BET bromodomain inhibitors. Here, we report the first identification of a ligandable site on a bromodomain outside the acetyl-lysine binding site. Inspired by our computational prediction of hotspots adjacent to non-homologous cysteine residues within the <i>C</i>-terminal Brd4 bromodomain (Brd4-BD2), we performed a mid-throughput mass spectrometry screen to identify cysteine-reactive fragments that covalently and selectively modify Brd4. Subsequent mass spectrometry, NMR and computational docking analyses of electrophilic fragment hits revealed a novel ligandable site near Cys356 that is unique to Brd4 among all human bromodomains. This site is orthogonal to the Brd4-BD2 acetyl-lysine binding site as Cys356 modification did not impact binding of the pan-BET bromodomain inhibitor JQ1 in fluorescence polarization assays. Finally, we tethered covalent fragments to JQ1 and performed NanoBRET assays to provide proof of principle that this orthogonal site can be covalently targeted in intact human cells. Overall, we demonstrate the potential of targeting sites orthogonal to bromodomain acetyl-lysine binding sites to develop bivalent and covalent inhibitors that displace Brd4 from chromatin.</p>

scholarly journals Mass spectrometry‐based top‐down and bottom‐up approaches for proteomic analysis of the Moroccan Buthus occitanus scorpion venom

FEBS Open Bio ◽  
2021 ◽  
Author(s):  
Khadija Daoudi ◽  
Christian Malosse ◽  
Ayoub Lafnoune ◽  
Bouchra Darkaoui ◽  
Salma Chakir ◽  
...  
Keyword(s):  
Mass Spectrometry ◽  
Proteomic Analysis ◽  
Scorpion Venom ◽  
Top Down ◽  
Bottom Up

scholarly journals The Analysis of Bayer Liquor by SPME-GC-MS of Derivatized Organic Poisons

Proceedings ◽  
2021 ◽  
Vol 57 (1) ◽  
pp. 101
Author(s):  
Virgil Badescu ◽  
Raluca Senin
Keyword(s):  
Mass Spectrometry ◽  
Gas Chromatography ◽  
Gas Chromatography Mass Spectrometry ◽  
Bayer Liquor ◽  
Chromatography Mass Spectrometry ◽  
Ms Analysis ◽  
Silylating Agent

The aim of this article was the gas chromatography–mass spectrometry (GC-MS) analysis oforganic matter from a residual liquor sample (S.C. Alum S.A., Tulcea), extracted by the solid-phasemicroextraction method (SPMA) and derivatized with N-(tert-butyldimethylsilyl)-Nmethyltrifluoroacetamide(MTBSTFA) as the silylating agent. [...]

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