A new peptidic vector for molecular imaging of apoptosis, identified by phage display technology
A new peptidic vector for molecular imaging of apoptosis, identified by phage display technology
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DOI：
10.1177/1087057106288220
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发表时间：
2006-08-01
影响因子：
--
通讯作者：
Muller, Robert N.
中科院分区：
文献类型：
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作者：
Laumonier, Catherine;Segers, Jerome;Muller, Robert N.
磷脂酰丝氨酸（PS）暴露于细胞表面是细胞凋亡的早期标志。为了选择PS结合肽作为造影剂载体来成像细胞凋亡，我们将噬菌体文库暴露在灌注的小鼠肝脏中。在第一次灌注时没有保留在对照肝脏上的噬菌体被用于在第二次灌注中选择凋亡的肝脏。进一步评估4个选定的噬菌体与ps包被酶联免疫吸附试验（ELISA）板的结合情况。它们对PS的表观亲和常数Ka （app）在6.08 × 10(10) M ~ 1.62 × 10(11) M之间。这些噬菌体不与磷脂酰胆碱结合，与膜联蛋白V的竞争证实了它们与PS的特异性相互作用。ELISA结果显示，与PS亲和系数最高的噬菌体Ka (app) = (1.6 +/- 0.2) × 10(11) M，它携带合成的TLVSSL肽。与膜联蛋白V和合成肽的特异性竞争证实了相互作用的特异性。
Phosphatidylserine (PS) exposure on the cell surface is an early marker of apoptosis. To select PS binding peptides as vectors of contrast agents to image apoptosis, a phage library has been exposed to perfused mouse livers. Phages not retained on control livers during the first perfusions were used for selections on apoptotic livers in a second series of perfusions. Four selected phages were further evaluated for binding to PS-coated enzyme-linked immunosorbent assay (ELISA) plates. They presented an apparent affinity constant (Ka (app)) for PS ranging from 6.08 x 10(10) M to 1.62 x 10(11) M. These phages did not bind to phosphatidylcholine, and competition with annexin V confirmed their specific interaction with PS. The phage with the highest affinity-bound PS in ELISA with a Ka (app) = (1.6 +/- 0.2) x 10(11) M. It carried the TLVSSL peptide that was synthesized. Specific competition with annexin V and with the synthetic peptide was performed and confirms the specificity of the interaction.