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@article{Achouba2025,

title = {Photoisomerization of Azobenzene‐Extended Charybdotoxin for the Optical Control of K_{v}1.2 Potassium Channel Activity},

author = {Yanis Achouba and Basile Peres and Steven Ascoët and Hervé Meudal and Cécile Caumes and Claude Zoukimian and Hugo Millet and Maureen Choteau‐Bodor and Cathy Carvalhosa and Mikael Croyal and Fella Bouchama and Heike Wulff and Stéphane Téletchéa and Rémy Béroud and Eléna Ishow and Céline Landon and Ahcène Boumendjel and Jérôme Montnach and Michel De Waard},

doi = {10.1002/anie.202423278},

issn = {1521-3773},

year  = {2025},

date = {2025-03-09},

urldate = {2025-03-09},

journal = {Angew Chem Int Ed},

publisher = {Wiley},

abstract = {<jats:title>Abstract</jats:title><jats:p>Natural peptides from animal venoms effectively modulate ion channel activity. While photoswitches regulate small compound pharmacology, their application to natural peptides rich in disulfide bridges and active on ion channels is novel due to larger pharmacophores. A pilot study integrating azobenzene photoswitches into charybdotoxin (ChTx), known for blocking potassium channels is initiated. Two click‐chemistry‐compatible azobenzene are synthesized differing in length and amide orientation (Az<jats:sub>1</jats:sub> & Az<jats:sub>2</jats:sub>). Az<jats:sub>1</jats:sub> is grafted onto ChTx at various amino acid positions using L‐azidohomoalanine mutation. ChTx monomers outperformed dimers, particularly with azobenzene at position 14, by exhibiting optimal photoswitching activity. In the <jats:italic>cis</jats:italic> configuration, Az<jats:sub>1</jats:sub> altered ChTx's pharmacophore, reducing potassium channel blockage, while conversely, Az<jats:sub>2</jats:sub> increased ChTx potency. This study pioneers photoswitch application to complex peptides, leveraging structure‐activity relationships. Successful integration depends on precise azobenzene positioning and chemical grafting guided by SAR insights. This advancement underscores the adaptability of photoswitch technology to intricate peptide structures, offering new avenues for pharmacological modulation.</jats:p>},

keywords = {},

pubstate = {published},

tppubtype = {article}

}

@article{Muñoz-Garcia2025,

title = {Interleukin-34 orchestrates bone formation through its binding to bone morphogenic proteins},

author = {Javier Muñoz-Garcia and Jorge W. Vargas-Franco and Kristina Schiavone and Marcus T. Keatinge and Robin Young and Jérôme Amiaud and Laurie Fradet and Jean-François Jégou and Hideo Yagita and Claudine Blin-Wakkach and Abdelilah Wakkach and Denis Cochonneau and Emilie Ollivier and Martine Pugière and Corinne Henriquet and Marie Legendre and Irina Giurgea and Serge Amselem and Marie-Françoise Heymann and Stéphane Télétchéa and Frédéric Lézot and Dominique Heymann},

url = {https://univ-poitiers.hal.science/hal-04901466/},

doi = {10.7150/thno.107340},

issn = {1838-7640},

year  = {2025},

date = {2025-02-11},

urldate = {2025-02-11},

journal = {Theranostics},

volume = {15},

number = {7},

pages = {3185--3202},

publisher = {Ivyspring International Publisher},

keywords = {},

pubstate = {published},

tppubtype = {article}

}

@article{Morot2025,

title = {Vibrio harveyi uses both type III secretion system and quorum sensing for the colonization of the European abalone},

author = {Amandine Morot and Christophe Lambert and Adeline Bidault and Alain Dufour and Sophie Rodrigues and François Delavat and Christine Paillard},

doi = {10.1016/j.fsi.2024.110103},

issn = {1050-4648},

year  = {2025},

date = {2025-02-00},

urldate = {2025-02-00},

journal = {Fish & Shellfish Immunology},

volume = {157},

publisher = {Elsevier BV},

keywords = {},

pubstate = {published},

tppubtype = {article}

}