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Artículos de revistas 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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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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2

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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11

Dengler, Sebastian, Ryan T. Howard, Vasily Morozov, et al. "Display Selection of a Hybrid Foldamer‐Peptide Macrocycle." Angewandte Chemie International Edition, September 14, 2023. http://dx.doi.org/10.1002/anie.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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12

Tran, Minh, Colby Parris, Carlos Esquivel, Andrea Oropeza, and Lei Wang. "The role of PPP1R3G in promoting kidney graft necroptosis during kidney transplantation." Physiology 40, S1 (2025). https://doi.org/10.1152/physiol.2025.40.s1.1378.

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Death of renal cells is central to the pathophysiology of kidney graft injury and delayed graft function in kidney transplant (KTX). Necroptosis, a recently discovered form of regulated cell death, has emerged as a pivotal event in the development of various kidney disorders, mainly triggered by the activation of receptor-interacting protein kinase 1 (RIPK1). Protein phosphatase 1 regulatory subunit 3G (PPP1R3G) has been identified to work with protein phosphatase 1γ (PP1γ) in kinase activation. However, the role of PPP1R3G in RIPK1 activation and tubular cell death remains unexplored. This st
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13

Loos, Manuel, Felix Xu, Pradeep K. Mandal, et al. "Interfacing B‐DNA and DNA Mimic Foldamers." Angewandte Chemie, May 9, 2025. https://doi.org/10.1002/ange.202505273.

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A linker unit was designed and synthesized that can serve both as a hairpin turn in a DNA duplex and anchor point for an aromatic helical foldamer mimicking the shape and surface properties of B‐DNA. Methods were developed to synthesize natural/non‐natural chimeric molecules combining foldamer and DNA segments. The ability of the linker to position the foldamer helix and the duplex DNA so that their rims and grooves are in register, despite their completely different chemical nature, was demonstrated using single crystal X‐ray diffraction, circular dichroism and molecular models. Bio‐layer int
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14

Loos, Manuel, Felix Xu, Pradeep K. Mandal, et al. "Interfacing B‐DNA and DNA Mimic Foldamers." Angewandte Chemie International Edition, May 9, 2025. https://doi.org/10.1002/anie.202505273.

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A linker unit was designed and synthesized that can serve both as a hairpin turn in a DNA duplex and anchor point for an aromatic helical foldamer mimicking the shape and surface properties of B‐DNA. Methods were developed to synthesize natural/non‐natural chimeric molecules combining foldamer and DNA segments. The ability of the linker to position the foldamer helix and the duplex DNA so that their rims and grooves are in register, despite their completely different chemical nature, was demonstrated using single crystal X‐ray diffraction, circular dichroism and molecular models. Bio‐layer int
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15

Puneeth Kumar, DRGKoppalu R., Zahid Manzoor Bhat, Sanjit Dey, et al. "Foldamer Nanotubes Mediated Label‐Free Detection of Protein‐Small Molecule Interactions." Chemistry – A European Journal, May 17, 2023. http://dx.doi.org/10.1002/chem.202300479.

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16

Simon, Márton A., Éva Bartus, Beáta Mag, et al. "Promiscuity mapping of the S100 protein family using a high-throughput holdup assay." Scientific Reports 12, no. 1 (2022). http://dx.doi.org/10.1038/s41598-022-09574-2.

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AbstractS100 proteins are small, typically homodimeric, vertebrate-specific EF-hand proteins that establish Ca2+-dependent protein–protein interactions in the intra- and extracellular environment and are overexpressed in various pathologies. There are about 20 distinct human S100 proteins with numerous potential partner proteins. Here, we used a quantitative holdup assay to measure affinity profiles of most members of the S100 protein family against a library of chemically synthetized foldamers. The profiles allowed us to quantitatively map the binding promiscuity of each member towards the fo
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