Abstract

Fatty acid binding proteins (FABPs) are proposed to function in the transport, metabolism, or storage of free fatty acids. Despite extensive studies, the mechanism of fatty acid binding and the ability of FABPs to discriminate among fatty acids according to their chain lengths and saturation state are poorly understood. In this work, we aimed to study the key features of FABP binding site based on the crystallographic structure of FABP-LCFA complexes, sequence multiple alignment and structural superposition of some FABPs. Due to the important role of the physicochemical features of the proteins in the ligand interaction, we studied those of the FABPs. The nature of the bond between the FABPs and the different LCFA, also the part of LCFA involved in LCFA-FABP interaction is interesting to detect the mechanism of LCFAs binding on FABPs. To achieve these objectives, we used different databases and various bioinformatics programs. Based on the results, we were able to answered some unclear about the mechanism of fatty acid binding.

Keywords:Long chain fatty acids; Fatty acid binding site; Multiple alignment; Similarity; Physicochemical characteristics