Peptides, Glycoconjugates and Metals in Biology

@article{Bachollet2020,
title = {Fluorogenic Protein Probes with Red and Near‐Infrared Emission for Genetically Targeted Imaging**},
author = {Sylvestre P J T Bachollet and Cyril Addi and Nicolas Pietrancosta and Jean-Maurice Mallet and Blaise Dumat},
url = {https://onlinelibrary.wiley.com/doi/abs/10.1002/chem.202002911 https://onlinelibrary.wiley.com/doi/10.1002/chem.202002911},
doi = {10.1002/chem.202002911},
issn = {0947-6539},
year = {2020},
date = {2020-11-01},
journal = {Chemistry \textendash A European Journal},
volume = {26},
number = {63},
pages = {14467--14473},
keywords = {},
pubstate = {published},
tppubtype = {article}
}

@article{Dumat2019,
title = {Mannose-Coated Fluorescent Lipid Microparticles for Specific Cellular Targeting and Internalization via Glycoreceptor-Induced Phagocytosis},
author = {Blaise Dumat and Lorraine Montel and L\'{e}a Pinon and Pascal Matton and Laurent Cattiaux and Jacques Fattaccioli and Jean-Maurice Mallet},
url = {https://pubs.acs.org/doi/10.1021/acsabm.9b00793},
doi = {10.1021/acsabm.9b00793},
issn = {2576-6422},
year = {2019},
date = {2019-11-01},
journal = {ACS Applied Bio Materials},
volume = {2},
pages = {5118-5126},
publisher = {American Chemical Society},
abstract = {In this work we report on the development of mannose-coated fluorescent lipid microparticles to study the role of C-type lectin membrane receptor in phagocytosis. The micrometric droplets of Soybean oil in water emulsion were functionalized with a tailor-made fluorescent mannolipid. The amphiphilic ligand was built from a mannose unit, a lipid C11 spacer and a naphthalimide fluorophore. The droplets functionalization was monitored by fluorescence microscopy as well as the interaction with concanavalin A which was used as a model lectin in vitro. The use of a monovalent ligand on the surface of emulsion droplets yielded particles with an affinity approximately 40 times higher than that of free mannose. In cellulo, the coated droplets were shown to be specifically internalized by macrophages in a receptor-dependent phagocytic pathway. The naked droplets on the other hand display very little internalization due to their low immunogenicity. This work thus brings evidence that C-type lectin membrane receptors ...},
keywords = {},
pubstate = {published},
tppubtype = {article}
}

@article{Bellier:2019,
title = {Methylglyoxal, a potent inducer of AGEs, connects between diabetes and cancer},
author = {J Bellier and M -J Nokin and E Lard\'{e} and P Karoyan and O Peulen and V Castronovo and A Bellahc\`{e}ne},
url = {https://www.scopus.com/inward/record.uri?eid=2-s2.0-85060445406&doi=10.1016%2fj.diabres.2019.01.002&partnerID=40&md5=0f0783fde807776888c9436e0430c762},
doi = {10.1016/j.diabres.2019.01.002},
year = {2019},
date = {2019-01-01},
journal = {Diabetes Research and Clinical Practice},
volume = {148},
pages = {200--211},
abstract = {Diabetes is one of the most frequent diseases throughout the world and its incidence is predicted to exponentially progress in the future. This metabolic disorder is associated with major complications such as neuropathy, retinopathy, atherosclerosis, and diabetic nephropathy, the severity of which correlates with hyperglycemia, suggesting that they are triggered by high glucose condition. Reducing sugars and reactive carbonyl species such as methylglyoxal (MGO) lead to glycation of proteins, lipids and DNA and the gradual accumulation of advanced glycation end products (AGEs) in cells and tissues. While AGEs are clearly implicated in the pathogenesis of diabetes complications, their potential involvement during malignant tumor development, progression and resistance to therapy is an emerging concept. Meta-analysis studies established that patients with diabetes are at higher risk of developing cancer and show a higher mortality rate than cancer patients free of diabetes. In this review, we highlight the potential connection between hyperglycemia-associated AGEs formation on the one hand and the recent evidence of pro-tumoral effects of MGO stress on the other hand. We also discuss the marked interest in anti-glycation compounds in view of their strategic use to treat diabetic complications but also to protect against augmented cancer risk in patients with diabetes. © 2019},
keywords = {},
pubstate = {published},
tppubtype = {article}
}

@article{Mazzoleni:2019,
title = {Glycoreplica peptides to investigate molecular mechanisms of immune-mediated physiological versus pathological conditions},
author = {A Mazzoleni and J -M Mallet and P Rovero and A M Papini},
url = {https://www.scopus.com/inward/record.uri?eid=2-s2.0-85059303265&doi=10.1016%2fj.abb.2018.12.030&partnerID=40&md5=054e28b7f9071c163b4af5dcba3d2fcd},
doi = {10.1016/j.abb.2018.12.030},
year = {2019},
date = {2019-01-01},
journal = {Archives of Biochemistry and Biophysics},
volume = {663},
pages = {44--53},
abstract = {Investigation of the role of saccharides and glycoconjugates in mechanisms of immune-mediated physiological and pathological conditions is a hot topic. In fact, in many autoimmune diseases cross-reactivity between sugar moieties exposed on exogenous pathogens and self-molecules has long been hinted. Several peptides have been reported as mimetics of glycans specifically interacting with sugar-binding antibodies. The seek for these glycoreplica peptides is instrumental in characterizing antigen mimicry pathways and their involvement in triggering autoimmunity. Therefore, peptides mimicking glycan-protein interactions are valuable molecular tools to overcome the difficulties of oligosaccharide preparations. The clinical impact of peptide-based probes for autoimmune diseases diagnosis and follow-up is emerging only recently as just the tip of the iceberg of an overlooked potential. Here we provide a brief overview of the relevance of the structural and functional aspects of peptide probes and their mimicry effect in autoimmunity mechanisms for promising applications in diagnostics and therapeutics. © 2019 Elsevier Inc.},
keywords = {},
pubstate = {published},
tppubtype = {article}
}

@article{Hu:2019,
title = {Electroactive fluorescent false neurotransmitter FFN102 partially replaces dopamine in PC12 cell vesicles},
author = {L Hu and A Savy and L Grimaud and M Guille-Collignon and F Lema\^{i}tre and C Amatore and J Delacotte},
url = {https://www.scopus.com/inward/record.uri?eid=2-s2.0-85057201704&doi=10.1016%2fj.bpc.2018.11.001&partnerID=40&md5=28655b4c152ce0fc51fc037feefcff97},
doi = {10.1016/j.bpc.2018.11.001},
year = {2019},
date = {2019-01-01},
journal = {Biophysical Chemistry},
volume = {245},
pages = {1--5},
abstract = {In the last decade, following fluorescent dyes and protein tags, pH sensitive false fluorescent neurotransmitters (FFN) were introduced and were valuable for labeling secretory vesicles and monitoring exocytosis at living cells. In particular, the synthetic analog of neurotransmitters FFN102 was shown to be an electroactive probe. Here, we show that FFN102 is suitable to be used as a bioanalytic probe at the widely used PC12 cell model. FFN102 was uptaken in the secretory vesicles of PC12 cells, partially replacing the endogenous dopamine stored in these vesicles. The different oxidation potentials of dopamine and FFN102 allowed to determine that ca. 12% of dopamine was replaced by FFN102. Moreover, the FFN102 was found to be over released through the initial fusion pore suggesting that it was mostly uptaken in fast diffusion compartment of the vesicles. © 2018 Elsevier B.V.},
keywords = {},
pubstate = {published},
tppubtype = {article}
}