Publications
15 results found
Calvo JS, Villones RLE, York NJ, et al., 2022, Evidence for a Long-Lived, Cu-Coupled and Oxygen-Inert Disulfide Radical Anion in the Assembly of Metallothionein-3 Cu(I)<sub>4</sub>-Thiolate Cluster, JOURNAL OF THE AMERICAN CHEMICAL SOCIETY, Vol: 144, Pages: 709-722, ISSN: 0002-7863
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- Citations: 10
Stefaniak E, Atrian-Blasco E, Goch W, et al., 2021, The Aggregation Pattern of Aβ<sub>1-40</sub> is Altered by the Presence of <i>N</i>-Truncated Aβ<sub>4-40</sub> and/or Cu<SUP>II</SUP> in a Similar Way through Ionic Interactions, CHEMISTRY-A EUROPEAN JOURNAL, Vol: 27, Pages: 2798-2809, ISSN: 0947-6539
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- Citations: 10
Stefaniak E, Pushie MJ, Vaerewyck C, et al., 2020, Exploration of the Potential Role for Aβ in Delivery of Extracellular Copper to Ctr1, INORGANIC CHEMISTRY, Vol: 59, Pages: 16952-16966, ISSN: 0020-1669
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- Citations: 5
Stefaniak E, Plonka D, Szczerba P, et al., 2020, Copper transporters? glutathione reactivity of products of Cu-A beta digestion by Neprilysin, Inorganic Chemistry: including bioinorganic chemistry, Vol: 59, Pages: 4186-4190, ISSN: 0020-1669
Aβ4–42 is the major subspecies of Aβ peptides characterized by avid Cu(II) binding via the ATCUN/NTS motif. It is thought to be produced in vivo proteolytically by neprilysin, but in vitro experiments in the presence of Cu(II) ions indicated preferable formation of C-terminally truncated ATCUN/NTS species including CuIIAβ4–16, CuIIAβ4–9, and also CuIIAβ12–16, all with nearly femtomolar affinities at neutral pH. Such small complexes may serve as shuttles for copper clearance from extracellular brain spaces, on condition they could survive intracellular conditions upon crossing biological barriers. In order to ascertain such possibility, we studied the reactions of CuIIAβ4–16, CuIIAβ4–9, CuIIAβ12–16, and CuIIAβ1–16 with reduced glutathione (GSH) under aerobic and anaerobic conditions using absorption spectroscopy and mass spectrometry. We found CuIIAβ4–16 and CuIIAβ4–9 to be strongly resistant to reduction and concomitant formation of Cu(I)–GSH complexes, with reaction times ∼10 h, while CuIIAβ12–16 was reduced within minutes and CuIIAβ1–16 within seconds of incubation. Upon GSH exhaustion by molecular oxygen, the CuIIAβ complexes were reformed with no concomitant oxidative damage to peptides. These finding reinforce the concept of Aβ4–x peptides as physiological trafficking partners of brain copper.
Teng X, Stefaniak E, Girvan P, et al., 2020, Hierarchical binding of copperII to N-truncated Aβ4-16 peptide, Metallomics: integrated biometal science, Vol: 12, Pages: 470-473, ISSN: 1756-5901
N-Truncated Aβ4–42 displays a high binding affinity with CuII. A mechanistic scheme of the interactions between Aβ4–42 and CuII has been proposed using a fluorescence approach. The timescales of different conversion steps were determined. This kinetic mechanism indicates the potential synaptic functions of Aβ4–42 during neurotransmission.
Fraczyk T, Bonna A, Stefaniak E, et al., 2020, Peptide Bond Cleavage by Ni(II) Ions within the Nuclear Localization Signal Sequence, CHEMISTRY & BIODIVERSITY, Vol: 17, ISSN: 1612-1872
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- Citations: 3
Pushie MJ, Stefaniak E, Sendzikr MR, et al., 2019, Using N-Terminal Coordination of Cu(II) and Ni(II) to Isolate the Coordination Environment of Cu(I) and Cu(II) Bound to His13 and His14 in Amyloid-β(4-16), INORGANIC CHEMISTRY, Vol: 58, Pages: 15138-15154, ISSN: 0020-1669
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- Citations: 15
Stefaniak E, Bal W, 2019, Cu<SUP>II</SUP> Binding Properties of N-Truncated Aβ Peptides: In Search of Biological Function, INORGANIC CHEMISTRY, Vol: 58, Pages: 13561-13577, ISSN: 0020-1669
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- Citations: 33
Stefaniak E, Plonka D, Drew SC, et al., 2018, The N-terminal 14-mer model peptide of human Ctr1 can collect Cu(ii) from albumin. Implications for copper uptake by Ctr1, METALLOMICS, Vol: 10, Pages: 1723-1727, ISSN: 1756-5901
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- Citations: 36
Santoro A, Wezynfeld NE, Stefaniak E, et al., 2018, Cu transfer from amyloid-<sub>4-16</sub> to metallothionein-3: the role of the neurotransmitter glutamate and metallothionein-3 Zn(ii)-load states, CHEMICAL COMMUNICATIONS, Vol: 54, Pages: 12634-12637, ISSN: 1359-7345
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- Citations: 19
Gonzalez P, Bossak K, Stefaniak E, et al., 2018, N-Terminal Cu-Binding Motifs (Xxx-Zzz-His, Xxx-His) and Their Derivatives: Chemistry, Biology and Medicinal Applications, CHEMISTRY-A EUROPEAN JOURNAL, Vol: 24, Pages: 8029-8041, ISSN: 0947-6539
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- Citations: 87
Bossak K, Drew SC, Stefaniak E, et al., 2018, The Cu(II) affinity of the N-terminus of human copper transporter CTR1: Comparison of human and mouse sequences, JOURNAL OF INORGANIC BIOCHEMISTRY, Vol: 182, Pages: 230-237, ISSN: 0162-0134
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- Citations: 24
Sendzik M, Pushie MJ, Stefaniak E, et al., 2017, Structure and Affinity of Cu(I) Bound to Human Serum Albumin, INORGANIC CHEMISTRY, Vol: 56, Pages: 15057-15065, ISSN: 0020-1669
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- Citations: 46
Wezynfeld NE, Stefaniak E, Stachucy K, et al., 2016, Resistance of Cu(Aβ4-16) to Copper Capture by Metallothionein-3 Supports a Function for the Aβ4-42 Peptide as a Synaptic Cu<SUP>II</SUP> Scavenger, ANGEWANDTE CHEMIE-INTERNATIONAL EDITION, Vol: 55, Pages: 8235-8238, ISSN: 1433-7851
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- Citations: 51
Fraczyk T, Zawisza IA, Goch W, et al., 2016, On the ability of CuAβ<sub>1-x</sub> peptides to form ternary complexes: Neurotransmitter glutamate is a competitor while not a ternary partner, JOURNAL OF INORGANIC BIOCHEMISTRY, Vol: 158, Pages: 5-10, ISSN: 0162-0134
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- Citations: 6
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