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 |
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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 | |
Publication status | Published - 25 Jan 2012 |