Bibliografías temáticas / Foldamer-Protein interaction

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Literatura académica sobre el tema "Foldamer-Protein interaction"

Autor: Grafiati
Publicado: 30 de noviembre de 2024
Última modificación: 31 de julio de 2025

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Artículos de revistas sobre el tema "Foldamer-Protein interaction"

1

Vallade, Maëlle, Post Sai Reddy, Lucile Fischer, and Ivan Huc. "Enhancing Aromatic Foldamer Helix Dynamics to Probe Interactions with Protein Surfaces." European Journal of Organic Chemistry 2018, no. 40 (2018): 5489–98. http://dx.doi.org/10.1002/ejoc.201800855.

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Tsuchiya, Keisuke, Takashi Kurohara, Kiyoshi Fukuhara, Takashi Misawa, and Yosuke Demizu. "Helical Foldamers and Stapled Peptides as New Modalities in Drug Discovery: Modulators of Protein-Protein Interactions." Processes 10, no. 5 (2022): 924. http://dx.doi.org/10.3390/pr10050924.

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A “foldamer” is an artificial oligomeric molecule with a regular secondary or tertiary structure consisting of various building blocks. A “stapled peptide” is a peptide with stabilized secondary structures, in particular, helical structures by intramolecular covalent side-chain cross-linking. Helical foldamers and stapled peptides are potential drug candidates that can target protein-protein interactions because they enable multipoint molecular recognition, which is difficult to achieve with low-molecular-weight compounds. This mini-review describes a variety of peptide-based foldamers and sta
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3

Suhonen, Aku, Heikki Laakkonen, and Maija Nissinen. "Structural effects of hinge length variation in a versatile foldamer backbone." Acta Crystallographica Section A Foundations and Advances 70, a1 (2014): C1719. http://dx.doi.org/10.1107/s2053273314082801.

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Foldamers are complex molecular scaffolds that mimic the form and function of biological molecules and are composed of simple repeating units.[1] Their potential applications include stereoselective and efficient organic catalysis mimicking the properties of enzymes, as well as bioreceptor mimics for new foldamer-protein interactions which could provide interesting possibilities for the medical industry.[2] In our previous studies we have investigated the folding properties of two oligoamides.[3] As the next step we prepared a series of aromatic oligoamide foldamers with several folding units
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4

Sadowsky, Jack D., W. Douglas Fairlie, Erik B. Hadley та ін. "(α/β+α)-Peptide Antagonists of BH3 Domain/Bcl-xLRecognition: Toward General Strategies for Foldamer-Based Inhibition of Protein−Protein Interactions". Journal of the American Chemical Society 129, № 1 (2007): 139–54. http://dx.doi.org/10.1021/ja0662523.

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5

Wéber, Edit, Péter Ábrányi-Balogh, Tamas A. Martinek, et al. "Target‐templated Construction of Functional Proteomimetics Using Photo‐foldamer Libraries." Angewandte Chemie International Edition, September 27, 2024. http://dx.doi.org/10.1002/anie.202410435.

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Current methods for proteomimetic engineering rely on structure‐based design. Here we describe a design strategy that allows the construction of proteomimetics against challenging targets without a priori characterization of the target surface. Our approach relies on (i) a 100‐membered photoreactive foldamer library, the members of which act as local surface mimetics, and (ii) the subsequent affinity maturation of the primary hits using systems chemistry. Two surface‐oriented proteinogenic side chains drove the interactions between the short helical foldamer fragments and the proteins. Diaziri
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6

Wéber, Edit, Péter Ábrányi-Balogh, Tamas A. Martinek, et al. "Target‐templated Construction of Functional Proteomimetics Using Photo‐foldamer Libraries." Angewandte Chemie, September 27, 2024. http://dx.doi.org/10.1002/ange.202410435.

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Current methods for proteomimetic engineering rely on structure‐based design. Here we describe a design strategy that allows the construction of proteomimetics against challenging targets without a priori characterization of the target surface. Our approach relies on (i) a 100‐membered photoreactive foldamer library, the members of which act as local surface mimetics, and (ii) the subsequent affinity maturation of the primary hits using systems chemistry. Two surface‐oriented proteinogenic side chains drove the interactions between the short helical foldamer fragments and the proteins. Diaziri
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7

Deepak, Deepak, Jiaojiao Wu, Valentina Corvaglia, et al. "DNA Mimic Foldamer Recognition of a Chromosomal Protein." Angewandte Chemie International Edition, December 23, 2024. https://doi.org/10.1002/anie.202422958.

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Helical aromatic oligoamide foldamers bearing anionic side chains that mimic the overall shape and charge surface distribution of DNA were synthesized. Their interactions with chromosomal protein Sac7d, a non‐sequence‐selective DNA‐binder that kinks DNA, were investigated by Surface Plasmon Resonance (SPR), Isothermal Titration Calorimetry (ITC), Circular Dichroism spectroscopy (CD), melting curve analysis, Atomic Force Microscopy (AFM), and Nuclear Magnetic Resonance (NMR), as well as by single crystal X‐ray crystallography. The foldamers were shown to bind to Sac7d better than a DNA duplex o
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8

Deepak, Deepak, Jiaojiao Wu, Valentina Corvaglia, et al. "DNA Mimic Foldamer Recognition of a Chromosomal Protein." Angewandte Chemie, December 23, 2024. https://doi.org/10.1002/ange.202422958.

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Helical aromatic oligoamide foldamers bearing anionic side chains that mimic the overall shape and charge surface distribution of DNA were synthesized. Their interactions with chromosomal protein Sac7d, a non‐sequence‐selective DNA‐binder that kinks DNA, were investigated by Surface Plasmon Resonance (SPR), Isothermal Titration Calorimetry (ITC), Circular Dichroism spectroscopy (CD), melting curve analysis, Atomic Force Microscopy (AFM), and Nuclear Magnetic Resonance (NMR), as well as by single crystal X‐ray crystallography. The foldamers were shown to bind to Sac7d better than a DNA duplex o
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9

Marković, Violeta, Jeelan Basha Shaik, Katarzyna Ożga, et al. "Peptide foldamer-based inhibitors of the SARS-CoV-2 S protein–human ACE2 interaction." Journal of Enzyme Inhibition and Medicinal Chemistry 38, no. 1 (2023). http://dx.doi.org/10.1080/14756366.2023.2244693.

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10

Dengler, Sebastian, Ryan T. Howard, Vasily Morozov, et al. "Display Selection of a Hybrid Foldamer‐Peptide Macrocycle." Angewandte Chemie, September 14, 2023. http://dx.doi.org/10.1002/ange.202308408.

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Expanding the chemical diversity of peptide macrocycle libraries for display selection is desirable to improve their potential at binding biomolecular targets. We now have implemented a considerable expansion through a large aromatic helical foldamer inclusion. A helical aromatic foldamer was identified that undergoes flexizyme‐mediated tRNA acylation and is capable of initiating ribosomal translation with yields sufficiently high to perform an mRNA display selection of macrocyclic foldamer‐peptide hybrids. A hybrid macrocyle nanomolar binder to the C‐lobe of the E6AP HECT domain was selected
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Tesis sobre el tema "Foldamer-Protein interaction"

1

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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2

Mbianda, Johanne. "Protein Surface Recognition with Urea-based foldamers : application to the design of ligands targeting histone chaperone proteins." Thesis, Bordeaux, 2018. http://www.theses.fr/2018BORD0184.

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Avec 8,8 millions de décès dénombrés en 2015, le cancer est l’une des plus grandes causes de mortalité dans le monde. De nouvelles stratégies thérapeutiques ont émergé et l’identification de nouvelles cibles biologiques comme notamment la protéine Asf1, un chaperon d’histone H3-H4 surexprimée dans les cellules cancéreuses et en particulier le cancer du sein. Cette protéine possède différentes fonctions dans la cellule et agit à plusieurs endroits par des interactions protéine-protéines. Au cours de cette thèse de doctorat, nous avons développé une stratégie originale de design d’inhibiteurs d’
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3

Buratto, Jeremie. "Reconnaissance de surfaces protéiques par des foldamères d'oligoamides aromatiques." Thesis, Bordeaux, 2014. http://www.theses.fr/2014BORD0003/document.

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Les interactions protéine - protéine sont au centre de nombreux processus biologiques, et représentent des cibles thérapeutiques pertinentes pour le traitement de certaines maladies. La conception de molécules antagonistes visant à inhiber ces interactions requiert la reconnaissance spécifique d’une des surfaces protéiques impliquées. Les foldamères de type oligoamides de quinoline constituent de bons candidats. Leur production et leur fonctionnalisation sont relativement aisées. Ils adoptent des structures hélicoïdales semblables à celles rencontrées dans les protéines. Grâce à différentes te
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