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首页> 外文期刊>Electrophoresis: The Official Journal of the International Electrophoresis Society >Study of binding stoichiometries of the human immunodeficiency virus type 1 reverse transcriptase by capillary electrophoresis and laser-induced fluorescence polarization using aptamers as probes.
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Study of binding stoichiometries of the human immunodeficiency virus type 1 reverse transcriptase by capillary electrophoresis and laser-induced fluorescence polarization using aptamers as probes.

机译：人类免疫缺陷病毒1型逆转录酶的结合化学计量学的研究通过毛细管电泳和激光诱导的荧光偏振，以适体为探针。

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摘要

Binding stoichiometries between four DNA aptamers (RT12, RT26, RTlt49, and ODN93) and the reverse transcriptase (RT) of the type 1 human immunodeficiency virus (HIV-1) were studied using affinity CE (ACE) coupled with LIF polarization and fluorescence polarization (FP). The ACE/LIF study showed evidence of two binding stoichiometries between the HIV-1 RT protein and aptamers RT12, RT26, and ODN93, suggesting that these aptamers can bind to both the p66 and p51 subunits of the HIV-1 RT. Only one binding stoichiometry for aptamer RTlt49 was found. The affinity complexes were easily separated from the unbound aptamers; however, the different stoichiometries were not well resolved. A complementary technique, FP, was able to provide additional information about the binding and supporting evidence for the ACE/LIF results. The ACE/LIFP study also revealed that the FP values of the 1:1 complexes of the HIV-1 RT protein with aptamers RT12, RT26, and ODN93 were always much greater than those of the 1:2 complexes. This was initially surprising because the larger molecular size of the 1:2 complexes was expected to result in higher FP values than the corresponding 1:1 complexes. This phenomenon was probably a result of fluorescence resonance energy transfer between the two fluorescent molecules bound to the HIV-1 RT protein.
机译：使用亲和CE（ACE）结合LIF极化和荧光极化研究了四种DNA适体（RT12，RT26，RTlt49和ODN93）与1型人类免疫缺陷病毒（HIV-1）的逆转录酶（RT）之间的结合化学计量（FP）。 ACE / LIF研究表明，在HIV-1 RT蛋白与适体RT12，RT26和ODN93之间存在两种结合化学计量的证据，表明这些适体可以与HIV-1 RT的p66和p51亚基结合。仅发现了适体RTlt49的一种结合化学计量。亲和复合物很容易与未结合的适体分离;然而，不同的化学计量并不能很好地解决。一项补充技术FP能够提供有关ACE / LIF结果的结合和支持证据的其他信息。 ACE / LIFP研究还显示，HIV-1 RT蛋白与适体RT12，RT26和ODN93的1：1配合物的FP值始终比1：2配合物大。最初这是令人惊讶的，因为与对应的1：1配合物相比，预期1：2配合物的分子尺寸更大会导致更高的FP值。这种现象可能是与HIV-1 RT蛋白结合的两个荧光分子之间荧光共振能量转移的结果。

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