Differential Interaction of Myoglobin with Select Fatty Acids of Carbon Chain Lengths C8 to C16.

Previous studies have shown that palmitic acid (PAM) and oleic acid (OLE) can bind myoglobin (Mb). How fatty acids (FA) with different carbon chain lengths and sulfate substitution interact with Mb remains uncertain. Indeed, C8:0 and C10:0 fatty acids do not perturb the intensities of the H-NMR MbCN signal intensity at FA:Mb ratios below 2:1. Starting with C12:0, C12:0-C16:0, FA induce a noticeable spectral change. C12:0 and C14:0 FA affect both the 5- and 8-heme methyl signals, whereas the C16:0 FA perturbs only the 8-heme methyl signal. All C12:0-C16:0 saturated FA induce upfield shifts in the -CH peak of different FA in the presence of Mb. Increasing the apparent solubility with a sulfate group substitution enhances the FA interaction of lauric sulfate (LAU 1-SO) but not palmitate sulfate acid (PAM 1-SO). The detergent (DET) property of FA has no significant contribution. Common positive, neutral, and negative DET at DET:Mb ratio of 1:1 induce no perturbation of the MbCN spectra. The experiment observations establish a basis to investigate the molecular mechanism underlying the FA interaction with Mb.