Relevant bibliographies by topics / Motif ATCUN

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  1. Journal articles
  2. Dissertations / Theses
  3. Book chapters

Academic literature on the topic 'Motif ATCUN'

Author: Grafiati
Published: 8 February 2025

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Journal articles on the topic "Motif ATCUN"

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Chen, Ruei-Ching, and Chung-Yu Lan. "Human Antimicrobial Peptide Hepcidin 25-Induced Apoptosis in Candida albicans." Microorganisms 8, no. 4 (April 17, 2020): 585. http://dx.doi.org/10.3390/microorganisms8040585.

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Hepcidin 25 (hep 25) is a cysteine-rich 25-amino acid antimicrobial peptide containing the amino-terminal Cu(II)/Ni(II)-binding (ATCUN) motif. Upon metal binding, the ATCUN motif is known to be involved in the generation of reactive oxygen species (ROS), especially hydrogen peroxide and hydroxyl radicals, which act against different bacterial species. However, the antifungal activity and its correlation to the Cu(II)-ATCUN complex of Hep 25 are still poorly understood. Here, we found that ROS accumulation plays an important role in the fungicidal activity of hep 25 against Candida albicans. In addition, Annexin V-FITC staining and TUNEL assay results provide clues about the apoptosis induced by hep 25. Moreover, hep 25 also increases the generation of ROS, possibly because of copper binding to the ATCUN motif, which is relevant to its activity against C. albicans. Finally, the C. albicans killing action of hep 25 is an energy- and temperature-dependent process that does not involve targeting the membrane. Taken together, our results provide new insights into the mechanisms of hep 25 against C. albicans cells and the potential use of hep 25 and its derivatives as novel antifungal agents.
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Miyamoto, Takaaki, Yuta Fukino, Shinichiro Kamino, Masashi Ueda, and Shuichi Enomoto. "Enhanced stability of Cu2+–ATCUN complexes under physiologically relevant conditions by insertion of structurally bulky and hydrophobic amino acid residues into the ATCUN motif." Dalton Transactions 45, no. 23 (2016): 9436–45. http://dx.doi.org/10.1039/c6dt01387b.

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Bacchella, Chiara, Simone Dell’Acqua, Stefania Nicolis, Enrico Monzani, and Luigi Casella. "Oxidase Reactivity of CuII Bound to N-Truncated Aβ Peptides Promoted by Dopamine." International Journal of Molecular Sciences 22, no. 10 (May 14, 2021): 5190. http://dx.doi.org/10.3390/ijms22105190.

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The redox chemistry of copper(II) is strongly modulated by the coordination to amyloid-β peptides and by the stability of the resulting complexes. Amino-terminal copper and nickel binding motifs (ATCUN) identified in truncated Aβ sequences starting with Phe4 show very high affinity for copper(II) ions. Herein, we study the oxidase activity of [Cu–Aβ4−x] and [Cu–Aβ1−x] complexes toward dopamine and other catechols. The results show that the CuII–ATCUN site is not redox-inert; the reduction of the metal is induced by coordination of catechol to the metal and occurs through an inner sphere reaction. The generation of a ternary [CuII–Aβ–catechol] species determines the efficiency of the oxidation, although the reaction rate is ruled by reoxidation of the CuI complex. In addition to the N-terminal coordination site, the two vicinal histidines, His13 and His14, provide a second Cu-binding motif. Catechol oxidation studies together with structural insight from the mixed dinuclear complexes Ni/Cu–Aβ4−x reveal that the His-tandem is able to bind CuII ions independently of the ATCUN site, but the N-terminal metal complexation reduces the conformational mobility of the peptide chain, preventing the binding and oxidative reactivity toward catechol of CuII bound to the secondary site.
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Magrì, Antonio, Giovanni Tabbì, Irina Naletova, Francesco Attanasio, Giuseppe Arena, and Enrico Rizzarelli. "A Deeper Insight in Metal Binding to the hCtr1 N-terminus Fragment: Affinity, Speciation and Binding Mode of Binuclear Cu2+ and Mononuclear Ag+ Complex Species." International Journal of Molecular Sciences 23, no. 6 (March 8, 2022): 2929. http://dx.doi.org/10.3390/ijms23062929.

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Ctr1 regulates copper uptake and its intracellular distribution. The first 14 amino acid sequence of the Ctr1 ectodomain Ctr1(1-14) encompasses the characteristic Amino Terminal Cu2+ and Ni2+ binding motif (ATCUN) as well as the bis-His binding motif (His5 and His6). We report a combined thermodynamic and spectroscopic (UV-vis, CD, EPR) study dealing with the formation of Cu2+ homobinuclear complexes with Ctr1(1-14), the percentage of which is not negligible even in the presence of a small Cu2+ excess and clearly prevails at a M/L ratio of 1.9. Ascorbate fails to reduce Cu2+ when bound to the ATCUN motif, while it reduces Cu2+ when bound to the His5-His6 motif involved in the formation of binuclear species. The histidine diade characterizes the second binding site and is thought to be responsible for ascorbate oxidation. Binding constants and speciation of Ag+ complexes with Ctr1(1-14), which are assumed to mimic Cu+ interaction with N-terminus of Ctr1(1-14), were also determined. A preliminary immunoblot assay evidences that the anti-Ctr1 extracellular antibody recognizes Ctr1(1-14) in a different way from the longer Ctr1(1-25) that encompasses a second His and Met rich domain.
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Neupane, Kosh P., Amanda R. Aldous, and Joshua A. Kritzer. "Macrocyclization of the ATCUN Motif Controls Metal Binding and Catalysis." Inorganic Chemistry 52, no. 5 (February 19, 2013): 2729–35. http://dx.doi.org/10.1021/ic302820z.

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6

Greve, Jenna M., and J. A. Cowan. "Activity and Synergy of Cu-ATCUN Antimicrobial Peptides." International Journal of Molecular Sciences 23, no. 22 (November 16, 2022): 14151. http://dx.doi.org/10.3390/ijms232214151.

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Antibiotic resistance demands innovative strategies and therapies. The pairs of antimicrobial peptides tested in this work show broad-spectrum synergy and are capable of interacting with diverse bacterial membranes. In most cases, the ATCUN motif enhanced the activity of peptides tested in combination. Our studies also show CP10A to be a multifaceted peptide, displaying both cell membrane and intracellular activity and acting as a chameleon, improving the activity of other peptides as needed. The results of the synergy experiments demonstrate the importance of varied modes of action and how these changes can affect the ability to combat pathogens, while also illustrating the value of the metal-binding domain in enhancing the activity of antimicrobial peptides in combination.
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Santoro, Alice, Gulshan Walke, Bertrand Vileno, Prasad P. Kulkarni, Laurent Raibaut, and Peter Faller. "Low catalytic activity of the Cu(ii)-binding motif (Xxx-Zzz-His; ATCUN) in reactive oxygen species production and inhibition by the Cu(i)-chelator BCS." Chemical Communications 54, no. 84 (2018): 11945–48. http://dx.doi.org/10.1039/c8cc06040a.

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Mital, Mariusz, Kosma Szutkowski, Karolina Bossak-Ahmad, Piotr Skrobecki, Simon C. Drew, Jarosław Poznański, Igor Zhukov, Tomasz Frączyk, and Wojciech Bal. "The Palladium(II) Complex of Aβ4−16 as Suitable Model for Structural Studies of Biorelevant Copper(II) Complexes of N-Truncated Beta-Amyloids." International Journal of Molecular Sciences 21, no. 23 (December 2, 2020): 9200. http://dx.doi.org/10.3390/ijms21239200.

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The Aβ4−42 peptide is a major beta-amyloid species in the human brain, forming toxic aggregates related to Alzheimer’s Disease. It also strongly chelates Cu(II) at the N-terminal Phe-Arg-His ATCUN motif, as demonstrated in Aβ4−16 and Aβ4−9 model peptides. The resulting complex resists ROS generation and exchange processes and may help protect synapses from copper-related oxidative damage. Structural characterization of Cu(II)Aβ4−x complexes by NMR would help elucidate their biological function, but is precluded by Cu(II) paramagneticism. Instead we used an isostructural diamagnetic Pd(II)-Aβ4−16 complex as a model. To avoid a kinetic trapping of Pd(II) in an inappropriate transient structure, we designed an appropriate pH-dependent synthetic procedure for ATCUN Pd(II)Aβ4−16, controlled by CD, fluorescence and ESI-MS. Its assignments and structure at pH 6.5 were obtained by TOCSY, NOESY, ROESY, 1H-13C HSQC and 1H-15N HSQC NMR experiments, for natural abundance 13C and 15N isotopes, aided by corresponding experiments for Pd(II)-Phe-Arg-His. The square-planar Pd(II)-ATCUN coordination was confirmed, with the rest of the peptide mostly unstructured. The diffusion rates of Aβ4−16, Pd(II)-Aβ4−16 and their mixture determined using PGSE-NMR experiment suggested that the Pd(II) complex forms a supramolecular assembly with the apopeptide. These results confirm that Pd(II) substitution enables NMR studies of structural aspects of Cu(II)-Aβ complexes.
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Domergue, Jérémy, Pawel Guinard, Magali Douillard, Jacques Pécaut, Olivier Proux, Colette Lebrun, Alan Le Goff, Pascale Maldivi, Pascale Delangle, and Carole Duboc. "A Bioinspired NiII Superoxide Dismutase Catalyst Designed on an ATCUN-like Binding Motif." Inorganic Chemistry 60, no. 17 (August 20, 2021): 12772–80. http://dx.doi.org/10.1021/acs.inorgchem.1c00899.

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Ginotra, Yamini P., Shefali N. Ramteke, Rapole Srikanth, and Prasad P. Kulkarni. "Mass Spectral Studies Reveal the Structure of Aβ1–16–Cu2+Complex Resembling ATCUN Motif." Inorganic Chemistry 51, no. 15 (July 17, 2012): 7960–62. http://dx.doi.org/10.1021/ic301244x.

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Dissertations / Theses on the topic "Motif ATCUN"

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Zimmeter, Katharina. "Développement de sondes IRM à base de peptides ou thiosemicarbazones pour la détection de cuivre(II) dans le milieu physiologique." Electronic Thesis or Diss., Strasbourg, 2024. http://www.theses.fr/2024STRAF046.

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Le cuivre échangeable, principalement lié à l'albumine sérique humaine (HSA) dans le sang, est un biomarqueur potentiel pour des maladies comme celles de Wilson et d’Alzheimer. Aucune méthode spécifique pour le détecter in vivo n'existant à ce jour, cette thèse présente des avancées dans la conception de sondes IRM (imagerie par résonance magnétique) responsives au CuII via deux approches : les agents de contraste (AC) de type q et τR, intégrant chacun un complexe de gadolinium et un ligand spécifique du CuII. Une partie de la thèse est dédiée à la synthèse et à l’étude de ligands adaptés à ces deux approches avec une affinité et une sélectivité suffisantes pour le CuII : des dérivés du motif peptidique ATCUN pour les sondes de type q et des α-pyridyl-thiosemicarbazones pour les sondes de type τR. L'autre partie porte sur leur association avec des agents IRM et leur caractérisation. Les sondes étudiées ont validé le principe des deux approches, bien que des optimisations restent nécessaires. Une relaxivité accrue de presque 400% a été observée pour l'AC de type q, DO3A-pyrGH, en présence de CuII, et une augmentation faible, mais notable pour les sondes τR en présence simultanée de CuII et de HSA
Exchangeable copper, which is primarily bound to human serum albumin (HSA) in the blood, is a potential biomarker for diseases such as Wilson's and Alzheimer's. To date, there is no specific method for its detection in vivo. This thesis presents progress in the design of CuII-responsive MRI (magnetic resonance imaging) probes through two approaches: q-based and τR-based contrast agents (CAs), each containing a gadolinium complex and a CuII-specific ligand. One part of the work is dedicated to the development of ligands adapted to these two approaches, with sufficient CuII-affinity and selectivity: derivatives of the peptidic ATCUN motif for q-based probes and α-pyridyl thiosemicarbazones for τR-based probes. The other part focuses on their incorporation into MRI CAs and their characterization. The probes studied proved the principle of both approaches, although optimizations are still needed. An increase in relaxivity of nearly 400% was observed for the q-based CA, DO3A-pyrGH, in the presence of CuII, and a small but notable increase for τR-type probes in the simultaneous presence of CuII and HSA
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Bradford, Seth Stephen. "The Design and Evaluation of Catalytic MetalloDrugs Targeting HCV IRES RNA: Demonstration of a New Therapeutic Approach." The Ohio State University, 2012. http://rave.ohiolink.edu/etdc/view?acc_num=osu1345132549.

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Book chapters on the topic "Motif ATCUN"

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Sarkar, B. "Design of Proteins with ATCUN Motif which Specifically Cleave DNA." In Cytotoxic, Mutagenic and Carcinogenic Potential of Heavy Metals Related to Human Environment, 477–91. Dordrecht: Springer Netherlands, 1997. http://dx.doi.org/10.1007/978-94-011-5780-3_30.

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Yu, Zhen, and James A. Cowan. "Design and applications of catalytic metallodrugs containing the ATCUN motif." In Medicinal Chemistry, 361–91. Elsevier, 2020. http://dx.doi.org/10.1016/bs.adioch.2019.10.005.

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