Peptides, Glycoconjugates and Metals in Biology

@article{molecules27175476,
title = {Improvement of Peptidyl Copper Complexes Mimicking Catalase: A Subtle Balance between Thermodynamic Stability and Resistance towards H2O2 Degradation},
author = {Yaqine Ben Hadj Hammouda and Koudedja Coulibaly and Alimatou Bathily and Magdalene Teoh Sook Han and Clotilde Policar and Nicolas Delsuc},
url = {https://www.mdpi.com/1420-3049/27/17/5476},
doi = {10.3390/molecules27175476},
issn = {1420-3049},
year = {2022},
date = {2022-01-01},
journal = {Molecules},
volume = {27},
number = {17},
abstract = {Catalase mimics are low molecular weight metal complexes that reproduce the activity of catalase, an antioxidant metalloprotein that participates in the cellular regulation of H2O2 concentration by catalyzing its dismutation. H2O2 is a reactive oxygen species that is vital for the normal functioning of cells. However, its overproduction contributes to oxidative stress, which damages cells. Owing to their biocompatibility, peptidyl complexes are an attractive option for clinical applications to regulate H2O2 by enzyme mimics. We report here the synthesis and characterization of four new peptidyl di-copper complexes bearing two coordinating sequences. Characterization of the complexes showed that, depending on the linker used between the two coordinating sequences, their catalytic activity for H2O2 dismutation, their thermodynamic stability and their resistance to H2O2 degradation are very different, with (CATm2)Cu2 being the most promising catalyst.},
keywords = {},
pubstate = {published},
tppubtype = {article}
}

@article{Bachollet2022b,
title = {Fluorogenic and Genetic Targeting of a Red-Emitting Molecular Calcium Indicator},
author = {Sylvestre P J T Bachollet and Nicolas Pietrancosta and Jean-Maurice Mallet and Blaise Dumat},
doi = {10.1039/D2CC01792J},
year = {2022},
date = {2022-01-01},
journal = {Chemical Communications},
keywords = {},
pubstate = {published},
tppubtype = {article}
}

@article{Bachollet2022,
title = {An expanded palette of fluorogenic HaloTag probes with enhanced contrast for targeted cellular imaging},
author = {Sylvestre P J T Bachollet and Yuriy Shpinov and Fanny Broch and Hela Benaissa and Arnaud Gautier and Nicolas Pietrancosta and Jean-Maurice Mallet and Blaise Dumat},
url = {http://xlink.rsc.org/?DOI=D1OB02394B},
doi = {10.1039/D1OB02394B},
issn = {1477-0520},
year = {2022},
date = {2022-01-01},
journal = {Organic & Biomolecular Chemistry},
volume = {20},
number = {17},
pages = {3619 - 3628},
publisher = {Royal Society of Chemistry},
abstract = {A palette of fluorogenic molecular rotor probes with emissions from green to NIR was developed for wash-free and multicolor imaging of genetically-encoded HaloTag fusion proteins.},
keywords = {},
pubstate = {published},
tppubtype = {article}
}

@article{schanne_inertness_2022,
title = {Inertness of Superoxide Dismutase Mimics Mn(II) Complexes Based on an Open-Chain Ligand, Bioactivity, and Detection in Intestinal Epithelial Cells},
author = {Gabrielle Schanne and Martha Zoumpoulaki and G\'{e}raldine Gazzah and Amandine Vincent and Hugues Preud’homme and Ryszard Lobinski and Sylvie Demignot and Philippe Seksik and Nicolas Delsuc and Clotilde Policar},
url = {https://www.hindawi.com/journals/omcl/2022/3858122/},
doi = {10.1155/2022/3858122},
issn = {1942-0900},
year = {2022},
date = {2022-01-01},
urldate = {2022-04-03},
journal = {Oxidative Medicine and Cellular Longevity},
volume = {2022},
pages = {e3858122},
abstract = {Oxidative stress is known to play a major role in the pathogenesis of inflammatory bowel diseases (IBDs), and, in particular, superoxide dismutase (SODs) defenses were shown to be weakened in patients suffering from IBDs. SOD mimics, also called SOD mimetics, as low-molecular-weight complexes reproducing the activity of SOD, constitute promising antioxidant catalytic metallodrugs in the context of IBDs. A Mn(II) complex SOD mimic (Mn1) based on an open-chain diaminoethane ligand exerting antioxidant and anti-inflammatory effects on an intestinal epithelial cellular model was shown to experience metal exchanges between the manganese center and metal ions present in the biological environment (such as Zn(II)) to some degrees. As the resulting complexes (mainly Zn(II)) were shown to be inactive, improving the kinetic inertness of Mn(II) complexes based on open-chain ligands is key to improve their bioactivity in a cellular context. We report here the study of three new Mn(II) complexes resulting from Mn1 functionalization with a cyclohexyl and/or a propyl group meant to limit, respectively, (a) metal exchanges and (b) deprotonation of an amine from the 1,2-diaminoethane central scaffold. The new manganese-based SOD mimics display a higher intrinsic SOD activity and also improved kinetic inertness in metal ion exchange processes (with Zn(II), Cu(II), Ni(II), and Co(II)). They were shown to provide anti-inflammatory and antioxidant effects in cells at lower doses than Mn1 (down to 10 μM). This improvement was due to their higher inertness against metal-assisted dissociation and not to different cellular overall accumulations. Based on its higher inertness, the SOD mimic containing both the propyl and the cyclohexyl moieties was suitable for intracellular detection and quantification by mass spectrometry, quantification, that was achieved by using a 13C-labeled Co-based analog of the SOD mimics as an external heavy standard.},
note = {Publisher: Hindawi},
keywords = {},
pubstate = {published},
tppubtype = {article}
}

@article{https://doi.org/10.1002/anie.202203066,
title = {Deciphering the Metal Speciation in Low-Molecular-Weight Complexes by IMS-MS: Application to the Detection of Manganese Superoxide Dismutase Mimics in Cell Lysates},
author = {Martha Zoumpoulaki and Gabrielle Schanne and Nicolas Delsuc and Hugues Preud'homme and Elodie Qu\'{e}vrain and Nicolas Eskenazi and G\'{e}raldine Gazzah and Regis Guillot and Philippe Seksik and Joelle Vinh and Ryszard Lobinski and Clotilde Policar},
url = {https://onlinelibrary.wiley.com/doi/abs/10.1002/anie.202203066},
doi = {https://doi.org/10.1002/anie.202203066},
year = {2022},
date = {2022-01-01},
journal = {Angewandte Chemie International Edition},
volume = {n/a},
number = {n/a},
pages = {e202203066},
abstract = {Abstract The detection and quantification of exogenous metal complexes are crucial to understanding their activity in intricate biological media. MnII complexes are difficult to detect and quantify because of low association constants, and high lability. The superoxide dismutase (SOD) mimic (or mimetic) labelled Mn1 is based on a 1,2-di-aminoethane functionalized with imidazole and phenolate and has good intrinsic anti-superoxide, antioxidant and anti-inflammatory activities in lipopolysaccharide (LPS)-activated intestinal epithelial HT29-MD2 cells, similar to that of its propylated analogue labelled Mn1P. Ion mobility spectrometry-mass spectrometry (IMS-MS) is a powerful technique for separating low molecular weight (LMW) metal complexes and can even separate complexes with the same ligand but bound to different divalent metal cations with similar ionic radii. We demonstrated the intracellular presence of the Mn1 and Mn1P complexes, at least partly intact, in lysates of cells incubated with the complexes and estimated the intracellular Mn1P concentration using a Co-13C6 analogue.},
keywords = {},
pubstate = {published},
tppubtype = {article}
}