The copper binding properties of metformin - QCM-D, XPS and nanobead agglomeration

Xueling Quan; Rokon Uddin; Arto Heiskanen; Mattias Parmvi; Katharina Nilson; Marco Donolato; Mikkel Fougt Hansen; Graham Rena; Anja Boisen

doi:10.1039/c5cc04321b

The copper binding properties of metformin - QCM-D, XPS and nanobead agglomeration

Xueling Quan, Rokon Uddin, Arto Heiskanen, Mattias Parmvi, Katharina Nilson, Marco Donolato, Mikkel Fougt Hansen, Graham Rena, Anja Boisen

University of Dundee

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Abstract

Study of the copper binding properties of metformin is important for revealing its mechanism of action as a first-line type-2 diabetes drug. A quantitative investigation of interactions between metformin and l-cysteine-copper complexes was performed. The results suggest that metformin could interact with biological copper, which plays a key role in mitochondrial function.

Original language	English
Journal	Chemical Communications
Volume	51
Issue number	97
Pages (from-to)	17313-17316
ISSN	1359-7345
DOIs	https://doi.org/10.1039/c5cc04321b
Publication status	Published - 2015

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abstract = "Study of the copper binding properties of metformin is important for revealing its mechanism of action as a first-line type-2 diabetes drug. A quantitative investigation of interactions between metformin and l-cysteine-copper complexes was performed. The results suggest that metformin could interact with biological copper, which plays a key role in mitochondrial function. ",

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AU - Uddin, Rokon

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AU - Nilson, Katharina

AU - Donolato, Marco

AU - Hansen, Mikkel Fougt

AU - Rena, Graham

AU - Boisen, Anja

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AB - Study of the copper binding properties of metformin is important for revealing its mechanism of action as a first-line type-2 diabetes drug. A quantitative investigation of interactions between metformin and l-cysteine-copper complexes was performed. The results suggest that metformin could interact with biological copper, which plays a key role in mitochondrial function.

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DO - 10.1039/c5cc04321b

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The copper binding properties of metformin - QCM-D, XPS and nanobead agglomeration

Abstract

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