Relevant bibliographies by topics / Fluorinated foldamers

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  1. Journal articles
  2. Dissertations / Theses
  3. Conference papers

Academic literature on the topic 'Fluorinated foldamers'

Author: Grafiati
Published: 30 November 2024
Last updated: 31 July 2025

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Journal articles on the topic "Fluorinated foldamers"

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Laxio Arenas, José, Yaochun Xu, Thierry Milcent, et al. "Fluorinated Triazole Foldamers: Folded or Extended Conformational Preferences." ChemPlusChem 86, no. 2 (2021): 241–51. http://dx.doi.org/10.1002/cplu.202000791.

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Cayrou, Chloé, Astrid Walrant, Delphine Ravault, et al. "Incorporation of CF3-pseudoprolines into polyproline type II foldamers confers promising biophysical features." Chemical Communications, 2024. http://dx.doi.org/10.1039/d4cc02895c.

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The development and the use of fluorinated polyproline-type II (PPII) foldamers are still underexplored. Herein, trifluoromethyl pseudoprolines have been incorporated into polyproline backbones without affecting their PPII helicity. The ability...
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Laxio Arenas, José, Jacopo Lesma, Tap Ha-Duong, et al. "Relation between conformation and activity on islet amyloid polypeptide aggregation of fluorinated foldamers based on N‐difluoromethyl‐1,4‐triazole amino acids." Chemistry – A European Journal, March 13, 2024. http://dx.doi.org/10.1002/chem.202303887.

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Novel fluorinated foldamers based on aminomethyl‐1,4‐triazolyl‐difluoroacetic acid (1,4‐Tz‐CF2) units were synthesized and their conformational behaviour was studied by NMR and molecular dynamics. Their activity on the aggregation of the human islet amyloid polypeptide (hIAPP) amyloid protein was evaluated by fluorescence spectroscopy and mass spectrometry. The fluorine labelling of these foldamers allowed the analysis of their interaction with the target protein. We demonstrated that the preferred extended conformation of homotriazolamers of 1,4‐Tz‐CF2 unit increases the aggregation of hIAPP,
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4

Picois, Nathan, Lizeth Bodero, Pierre Milbeo, Thierry Brigaud та Grégory Chaume. "Bimodal use of chiral α‐Trifluoromethylalanine in Aib Foldamers: study of the position impact towards the helical screw‐sense preference". Chemistry – A European Journal, 6 березня 2024. http://dx.doi.org/10.1002/chem.202400540.

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Oligomers of the achiral α‐aminoisobutyric acid (Aib) adopt a 310 helical conformation in which the screw‐sense preference can be controlled by a single chiral residue. The use of the fluorinated residue α‐Trifluoromethylalanine (α‐TfmAla) revealed a unique way to both induce and measure the screw‐sense preference of such oligomers acting as 19F NMR probe. This work proposes a systematic study of the effect of this fluorinated chiral inducer on the helical screw‐sense preference of poly‐Aib oligomers. The impact of the position of the fluorinated residue into pentamers (N‐terminal, central or
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Doerner, Benedicte, Flavio della Sala, Siyuan Wang, and Simon John Webb. "Reaction, Recognition, Relay: Anhydride Hydrolysis Reported by Conformationally Responsive Fluorinated Foldamers in Micelles." Angewandte Chemie International Edition, May 4, 2024. http://dx.doi.org/10.1002/anie.202405924.

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Natural membrane receptors are proteins that can report on changes in the concentration of external chemical messengers. Messenger binding to a receptor produces conformational changes that are relayed through the membrane into the cell; this information allows cells to adapt to changes in their environment. Artificial membrane receptors (R)‐1 and (S)‐1 are helical α‐aminoisobutyric acid (Aib) foldamers that replicate key parts of this information relay. Solution‐phase 19F NMR spectroscopy of zinc(II)‐capped receptor 1, either in organic solvent or in membrane‐mimetic micelles, showed messenge
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Doerner, Benedicte, Flavio della Sala, Siyuan Wang, and Simon John Webb. "Reaction, Recognition, Relay: Anhydride Hydrolysis Reported by Conformationally Responsive Fluorinated Foldamers in Micelles." Angewandte Chemie, May 4, 2024. http://dx.doi.org/10.1002/ange.202405924.

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Natural membrane receptors are proteins that can report on changes in the concentration of external chemical messengers. Messenger binding to a receptor produces conformational changes that are relayed through the membrane into the cell; this information allows cells to adapt to changes in their environment. Artificial membrane receptors (R)‐1 and (S)‐1 are helical α‐aminoisobutyric acid (Aib) foldamers that replicate key parts of this information relay. Solution‐phase 19F NMR spectroscopy of zinc(II)‐capped receptor 1, either in organic solvent or in membrane‐mimetic micelles, showed messenge
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Dissertations / Theses on the topic "Fluorinated foldamers"

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Cayrou, Chloé. "Conception, Synthèse et Analyse Structurale de Foldamères Fluorés de Conformation Hélicoïdale Polyproline de type II Ciblant des Membranes ou des Protéines Amyloïdes." Electronic Thesis or Diss., CY Cergy Paris Université, 2024. http://www.theses.fr/2024CYUN1308.

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Le terme foldamère désigne tout oligomère capable de se replier en une structure conformationnellement stable en solution. Parmi eux, les foldamères peptidiques semblent particulièrement intéressants pour répondre à plusieurs défis rencontrés avec les peptides en chimie médicinale, tels que leur trop grande flexibilité et leur faible stabilité in vivo. Le caractère structuré des foldamères peut ainsi s’avérer être un atout dans le développement de nouveaux peptides d’intérêt biologique interagissant avec des protéines ou des membranes (Peptides de Pénétration Cellulaire, CPPs ou Peptides AntiM
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Picois, Nathan. "Incorporation d’acides aminés trifluorométhylés quaternaires pour la quantification et le contrôle de la structure secondaire d’architectures moléculaires." Electronic Thesis or Diss., CY Cergy Paris Université, 2024. http://www.theses.fr/2024CYUN1296.

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Les oligomères d’acide α aminoisobutyrique (Aib) sont connus pour se structurer en hélices 310 stables. Ces oligomères présentent un ratio 1:1 d’hélice gauche et droite résultant du caractère achiral de l’Aib. Par introduction d’un résidu chiral nommé contrôleur au sein de la chaîne peptidique, un sens d’hélicité préférentiel gauche ou droit est induit. Le sens d’hélicité est alors attribué par dichroïsme circulaire et peut être quantifié par l’intermédiaire d’un reporteur RMN présent dans la chaîne peptidique. Ces systèmes ont fait l’objet de nombreuses études pour rendre compte de la capacit
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3

Bordessa, Andrea. "Design, synthesis and structural evaluation of peptidomimetics towards foldamers, PNAs and non covalent inhibitors of the 20S proteasome." kostenfrei, 2008. http://www.opus-bayern.de/uni-regensburg/volltexte/2009/1112/.

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Conference papers on the topic "Fluorinated foldamers"

1

Cayrou, Chloe, Simon Gonzalez, Astrid Walrant, et al. "Design and Structural Analysis of Fluorinated Polyproline-Type Foldamers and their Ability to Interact with Membrane Models." In 37th European Peptide Symposium. The European Peptide Society, 2024. http://dx.doi.org/10.17952/37eps.2024.p2064.

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