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Thermodynamics, structure, and antibacterial activity of the decavanadate-lysozyme complex

delete2026-06-06
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PRE
AI
O
Ola Grabowska
M
Martyna Kapica
A
Anna Kloska
K
Krzysztof Żamojć
A
Aleksandra Tesmar
M
Magdalena Zdrowowicz
S
Sergey A. Samsonov *
D
Dariusz Wyrzykowski *
DOI:10.1016/j.jinorgbio.2026.113383delete
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Abstract

Abstract

En 中文
• Stable 2:1 [V10O28]6−:lysozyme complex formed at pH 5.0 • Enthalpy-driven binding indicates dominant electrostatic interactions • MD simulations identify a single C-terminal binding site • Decavanadate binding induces major secondary structure changes • Synergistic antibacterial activity observed for the complex

Journal

Journal of Inorganic Biochemistry cover
Journal of Inorganic Biochemistry
IF:
3.2
Papers:
7.1K
Citations:
1.2W

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U
University of Gdansk
Scholars:
2.8K
Papers: 2.2K
Citations: 3.6K
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