Interaction of myoglobin with oleic acid.

Lifan Shih, Youngran Chung, Renuka Sriram, Thomas Jue

Chemistry and physics of lipids 2015 Oct

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Previous studies have shown that palmitate (PA) can interact with myoglobin (Mb). The present study has investigated the interaction of the more soluble unsaturated fatty acid, oleic acid (OA). Indeed, (1)H NMR measurements of the Mb signal during OA titration also show signal changes consistent with specific and non-specific binding. At OA:Mb ratio<4:1, OA perturbs selectively the 8-heme methyl signal, consistent with a local and specific fatty acid-protein interaction. As OA:Mb ratio increases from 4:1 to 40:1, all hyperfine shifted MbCN signals decrease, consistent with a non-selective, global perturbation of the protein. The pH titration analysis indicates that the observed OA methylene signal in the presence of Mb reflects a non-specific interaction and does not originate from a shift in the lamella-micelle equilibrium. Given the OA interaction with Mb, a fatty acid flux model suggests that Mb can play a fatty acid transport role under certain physiological conditions. Copyright © 2015 Elsevier Ireland Ltd. All rights reserved.

Citation

Lifan Shih, Youngran Chung, Renuka Sriram, Thomas Jue. Interaction of myoglobin with oleic acid. Chemistry and physics of lipids. 2015 Oct;191:115-22