Stabilization and Binding of [V4O12]4− and Unprecedented [V20O54(NO3)]n− to Lysozyme upon Loss of Ligands and Oxidation of the Potential Drug VIVO(acetylacetonato)2

Giarita Ferraro; Gabriella Tito; Giuseppe Sciortino; Eugenio Garribba; Antonello Merlino

doi:10.1002/anie.202310655

Stabilization and Binding of [V₄O₁₂]⁴⁻ and Unprecedented [V₂₀O₅₄(NO₃)]ⁿ⁻ to Lysozyme upon Loss of Ligands and Oxidation of the Potential Drug V^IVO(acetylacetonato)₂

Giarita Ferraro, Gabriella Tito, Giuseppe Sciortino, Eugenio Garribba^*, Antonello Merlino^*

^*Autor corresponent d’aquest treball

Departament de Química

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9 Cites (Scopus)

1 Descàrregues (Pure)

Resum

High-resolution crystal structures of lysozyme in the presence of the potential drug V^IVO(acetylacetonato)₂ under two different experimental conditions have been solved. The crystallographic study reveals the loss of the ligands, the oxidation of V^IV to V^V and the subsequent formation of adducts of the protein with two different polyoxidovanadates: [V₄O₁₂]⁴⁻, which interacts with lysozyme non-covalently, and the unprecedented [V₂₀O₅₄(NO₃)]ⁿ⁻, which is covalenty bound to the side chain of an aspartate residue of symmetry related molecules.

Idioma original	Anglès
Número d’article	e202310655
Nombre de pàgines	5
Revista	Angewandte Chemie - International Edition
Volum	62
Número	50
DOIs	https://doi.org/10.1002/anie.202310655
Estat de la publicació	Publicada - 11 de des. 2023

Accés al document

10.1002/anie.202310655

https://ddd.uab.cat/record/288503

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title = "Stabilization and Binding of [V4O12]4− and Unprecedented [V20O54(NO3)]n− to Lysozyme upon Loss of Ligands and Oxidation of the Potential Drug VIVO(acetylacetonato)2",

abstract = "High-resolution crystal structures of lysozyme in the presence of the potential drug VIVO(acetylacetonato)2 under two different experimental conditions have been solved. The crystallographic study reveals the loss of the ligands, the oxidation of VIV to VV and the subsequent formation of adducts of the protein with two different polyoxidovanadates: [V4O12]4−, which interacts with lysozyme non-covalently, and the unprecedented [V20O54(NO3)]n−, which is covalenty bound to the side chain of an aspartate residue of symmetry related molecules.",

keywords = "Lysozyme, Polyhedra, Polyoxidovanadates, Protein Interaction, Vanadium, Vanadium-Based Drugs",

author = "Giarita Ferraro and Gabriella Tito and Giuseppe Sciortino and Eugenio Garribba and Antonello Merlino",

note = "Publisher Copyright: {\textcopyright} 2023 The Authors. Angewandte Chemie International Edition published by Wiley-VCH GmbH.",

year = "2023",

month = dec,

day = "11",

doi = "10.1002/anie.202310655",

language = "English",

volume = "62",

journal = "Angewandte Chemie - International Edition",

issn = "1433-7851",

publisher = "John Wiley and Sons Ltd",

number = "50",

}

Stabilization and Binding of [V₄O₁₂]⁴⁻ and Unprecedented [V₂₀O₅₄(NO₃)]ⁿ⁻ to Lysozyme upon Loss of Ligands and Oxidation of the Potential Drug V^IVO(acetylacetonato)₂. / Ferraro, Giarita; Tito, Gabriella; Sciortino, Giuseppe et al.
In: Angewandte Chemie - International Edition, Vol. 62, Núm. 50, e202310655, 11.12.2023.

Producció científica: Contribució a revista › Article › Recerca › Avaluat per experts

TY - JOUR

T1 - Stabilization and Binding of [V4O12]4− and Unprecedented [V20O54(NO3)]n− to Lysozyme upon Loss of Ligands and Oxidation of the Potential Drug VIVO(acetylacetonato)2

AU - Ferraro, Giarita

AU - Tito, Gabriella

AU - Sciortino, Giuseppe

AU - Garribba, Eugenio

AU - Merlino, Antonello

PY - 2023/12/11

Y1 - 2023/12/11

N2 - High-resolution crystal structures of lysozyme in the presence of the potential drug VIVO(acetylacetonato)2 under two different experimental conditions have been solved. The crystallographic study reveals the loss of the ligands, the oxidation of VIV to VV and the subsequent formation of adducts of the protein with two different polyoxidovanadates: [V4O12]4−, which interacts with lysozyme non-covalently, and the unprecedented [V20O54(NO3)]n−, which is covalenty bound to the side chain of an aspartate residue of symmetry related molecules.

AB - High-resolution crystal structures of lysozyme in the presence of the potential drug VIVO(acetylacetonato)2 under two different experimental conditions have been solved. The crystallographic study reveals the loss of the ligands, the oxidation of VIV to VV and the subsequent formation of adducts of the protein with two different polyoxidovanadates: [V4O12]4−, which interacts with lysozyme non-covalently, and the unprecedented [V20O54(NO3)]n−, which is covalenty bound to the side chain of an aspartate residue of symmetry related molecules.

KW - Lysozyme

KW - Polyhedra

KW - Polyoxidovanadates

KW - Protein Interaction

KW - Vanadium

KW - Vanadium-Based Drugs

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DO - 10.1002/anie.202310655

M3 - Article

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SN - 1433-7851

VL - 62

JO - Angewandte Chemie - International Edition

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