Purity and Liposome Interaction of Drosophila Fatty Acid Binding Proteins

• Main Authors: Chou, Ching Yi, 周靜宜
• Other Authors: Lyu, Ping Chiang
• Format: Others
• Language: en_US
• Published: 2015
• Online Access: http://ndltd.ncl.edu.tw/handle/07151490755189193592

碩士 === 國立清華大學 === 生物資訊與結構生物研究所 === 104 === Drosophila melanogaster fatty acid binding protein (dFABP) is one of fatty acid binding protein family which belongs to intracellular lipid binding protein superfamily, a group of low molecular weight proteins, which binds to long chain fatty acids. FABPs express highly in mammalian and have tissue specificity. Physiological function of FABPs are reported to transport, metabolize and store fatty acid involving in energy storage, cell growth, cellular metabolism and so on. There are two hypotheses for interaction between FABPs and membranes, diffusional-dependent mechanism and collisional-dependent mechanism. In our previous studies, we characterized structural properties and fatty acid binding specificity of dFABP. But mechanism between dFABP and membranes remains unknown. As reports, the purification of FABPs easily accompanied with hydrophobic contamination even though delipidation was conducted. To measure the purity of dFABP, we used gas chromatography in this study to confirm the apo form of dFABP we obtained for further studies. This study aims to obtain pure apo form dFABP and investigate the relationship between dFABP and membranes by liposome titration experiment of nuclear magnetic resonance spectroscopy (NMR). We found interaction between apo form dFABP and liposome is strong. But interaction between holo form dFABP and liposome is weak. Altogether, we suggested phospholipid vesicles associated with apo form dFABP, but disassociated with holo form dFABP.