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Figure 11
Response of hFABP4 to fatty-acid and inhibitor binding. The inhibitors are the same as in Fig. 8[link]. The HSQC spectra are contoured at the same height for comparison. Apo hFABP4 (blue) strongly binds to bicelles (the same spectrum as in Fig. 9[link] for q = 0.75) and remains bound when oleic acid (black) is added. Upon the addition of a thiophene inhibitor (green), some detachment is apparent from the increased number and resolution of peaks. By contrast, the addition of linoleic acid (yellow) and a tetrazole inhibitor (magenta) lead to complete detachment of hFABP4 from micelles. The trend is also apparent from the 1D 1H NMR spectra, an enlarged version of which plus the corresponding orientations of Phe58 may be found in Supplementary Fig. S1. The line widths are smallest and the intensities are highest for linoleic acid and the tetrazole inhibitor, whereas for apo hFABP4 and oleic acid line broadening and bad peak resolution are strong. The thiophene inhibitor has intermediate properties.

Journal logoSTRUCTURAL
BIOLOGY
ISSN: 2059-7983
Volume 81| Part 8| August 2025| Pages 423-435
https://doi.org/10.1107/S2059798325006242
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