A molecular mechanism for modulating plasma Zn speciation by fatty acids

Jin Lu; Alan J. Stewart; Darrell Sleep; Peter J. Sadler; Teresa J. T. Pinheiro; Claudia A. Blindauer

doi:10.1021/ja210496n

A molecular mechanism for modulating plasma Zn speciation by fatty acids

Jin Lu, Alan J. Stewart, Darrell Sleep, Peter J. Sadler, Teresa J. T. Pinheiro, Claudia A. Blindauer

Research output: Contribution to journal › Article › peer-review

Abstract

Albumin transports both fatty acids and zinc in plasma. Competitive binding studied by isothermal titration calorimetry revealed that physiologically relevant levels of fatty acids modulate the Zn-binding capacity of albumin, with far-reaching implications for biological zinc speciation. The molecular mechanism for this effect is likely due to a large conformational change elicited by fatty acid binding to an high-affinity inter-domain site that disrupts at least one Zn site. Albumin may be a molecular device to "translate" certain aspects of the organismal energy state into global zinc signals.

Original language	English
Pages (from-to)	1454-1457
Number of pages	4
Journal	Journal of the American Chemical Society
Volume	134
Issue number	3
Early online date	4 Jan 2012
DOIs	https://doi.org/10.1021/ja210496n
Publication status	Published - 25 Jan 2012

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T1 - A molecular mechanism for modulating plasma Zn speciation by fatty acids

AU - Lu, Jin

AU - Stewart, Alan J.

AU - Sleep, Darrell

AU - Sadler, Peter J.

AU - Pinheiro, Teresa J. T.

AU - Blindauer, Claudia A.

PY - 2012/1/25

Y1 - 2012/1/25

N2 - Albumin transports both fatty acids and zinc in plasma. Competitive binding studied by isothermal titration calorimetry revealed that physiologically relevant levels of fatty acids modulate the Zn-binding capacity of albumin, with far-reaching implications for biological zinc speciation. The molecular mechanism for this effect is likely due to a large conformational change elicited by fatty acid binding to an high-affinity inter-domain site that disrupts at least one Zn site. Albumin may be a molecular device to "translate" certain aspects of the organismal energy state into global zinc signals.

AB - Albumin transports both fatty acids and zinc in plasma. Competitive binding studied by isothermal titration calorimetry revealed that physiologically relevant levels of fatty acids modulate the Zn-binding capacity of albumin, with far-reaching implications for biological zinc speciation. The molecular mechanism for this effect is likely due to a large conformational change elicited by fatty acid binding to an high-affinity inter-domain site that disrupts at least one Zn site. Albumin may be a molecular device to "translate" certain aspects of the organismal energy state into global zinc signals.

UR - http://ukpmc.ac.uk/articles/PMC3285120

UR - http://pubs.acs.org/doi/pdf/10.1021/ja210496n

U2 - 10.1021/ja210496n

DO - 10.1021/ja210496n

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SP - 1454

EP - 1457

JO - Journal of the American Chemical Society

JF - Journal of the American Chemical Society

IS - 3

ER -

A molecular mechanism for modulating plasma Zn speciation by fatty acids

Abstract

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