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首页> 外文期刊>Biochemistry >Binding of recombinant rat liver fatty acid-binding protein to small anionic phospholipid vesicles results in ligand release: a model for interfacial binding and fatty acid targeting.
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Binding of recombinant rat liver fatty acid-binding protein to small anionic phospholipid vesicles results in ligand release: a model for interfacial binding and fatty acid targeting.

机译：重组大鼠肝脏脂肪酸结合蛋白与小的阴离子磷脂囊泡的结合导致配体释放：界面结合和脂肪酸靶向的模型。

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摘要

A number of intracellular proteins bind to negatively charged phospholipid membranes, and this interfacial binding results in a conformational change that modulates the activity of the protein. Using a fluorescent fatty acid analogue, 11-[5-(dimethylamino)naphthalenesulfonyl]undecanoic acid (DAUDA), it is possible to demonstrate the release of this ligand from recombinant rat liver FABP in the presence of phospholipid vesicles that contain a significant proportion of anionic phospholipids. The ligand release that is observed with anionic phospholipids is sensitive to the ionic strength of the assay conditions and the anionic charge density of the phospholipid at the interface, indicating that nonspecific electrostatic interactions play an important role in the process. The stoichiometric relationship between anionic phospholipid and liver FABP suggests that the liver FABP coats the surface of the phospholipid vesicle. The most likely explanation for ligand release is that interaction of FABP with an anionic membrane interface induces a rapid conformational change, resulting in a reduced affinity of DAUDA for the protein. The nature of this interaction involves both electrostatic and nonpolar interactions as maximal release of liver FABP from phospholipid vesicles with recovery of ligand binding cannot be achieved with high salt and requires the presence of a nonionic detergent. The precise interfacial mechanism that results in the rapid release of ligand from L-FABP remains to be determined, but studies with two mutants, F3W and F18W, suggest the possible involvement of the amino-terminal region of the protein in the process. The conformational change linked to interfacial binding of this protein could provide a mechanism for fatty acid targeting within the cell.
机译：许多细胞内蛋白质与带负电荷的磷脂膜结合，这种界面结合导致构象变化，从而调节蛋白质的活性。使用荧光脂肪酸类似物11- [5-（5-（二甲基氨基）萘磺酰基]十一烷酸（DAUDA），可以证明在含有明显比例的磷脂囊泡的存在下，这种配体从重组大鼠肝脏FABP中的释放。阴离子磷脂。用阴离子磷脂观察到的配体释放对测定条件的离子强度和界面处磷脂的阴离子电荷密度敏感，表明非特异性静电相互作用在该过程中起重要作用。阴离子磷脂与肝脏FABP的化学计量关系表明，肝脏FABP覆盖了磷脂囊泡的表面。配体释放的最可能解释是FABP与阴离子膜界面的相互作用诱导了快速的构象变化，导致DAUDA对蛋白质的亲和力降低。这种相互作用的性质涉及静电和非极性相互作用，因为用高盐无法实现肝脏FABP从磷脂囊泡最大释放并恢复配体结合，并且需要存在非离子去污剂。导致配体从L-FABP快速释放的精确界面机制尚待确定，但是对F3W和F18W两个突变体的研究表明，该过程可能涉及蛋白质的氨基末端区域。与该蛋白的界面结合有关的构象变化可以为细胞内的脂肪酸靶向提供一种机制。

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