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Spectroscopic and Electrochemical Characterization of CD4 Binding Site of HIV-1 Exterior Envelope gp120

机译:HIV-1外包络GP120的CD4结合位点的光谱和电化学表征

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Glycoprotein 120 (gp120) is essential biomolecule for HIV-1 entry into cells as it plays a vital role inattachment to specific cell surface receptors. Exterior envelope glycoprotein 120 contains conservativeCD4 binding site in its structure that may be one of target molecules for development of HIVtherapeutic agents, able to inhibit the viral entry steps into the host cells. The present study describesthe solid-phase, Fmoc-based synthesis of CD4 binding site (SSGGD PEIVMH), and its subsequentspectroscopic characterization, with determined purity over 90 %. Moreover; electrochemical analyseswere carried out to optimize the conditions for peptide determination. Using the optimized conditionsas Britton-Robinson buffer with pH 8 and 3% addition of acetonitrile (v/v) as a mobile phase, potential-1 -11100 mV, limit of detection of 0.04 g.mL and limit of quantification of 0.1 g.mL were estimated.
机译:糖蛋白120(GP120)是用于HIV-1进入细胞的必需生物分子,因为它对特定细胞表面受体具有重要作用的重要作用。外壳糖蛋白120在其结构中含有保守的粘合位点,其结构可以是静脉内容性的靶分子之一,能够抑制进入宿主细胞的病毒进入步骤。本研究描述了CD4结合位点(SSGGD PEIVMH)的固相,FMOC基合成,其随后的光谱表征,纯度超过90%。而且;进行电化学分析,以优化肽测定条件。使用具有pH8和3%加入乙腈(v / v)的Britton-robinson缓冲液作为流动相,电位-1 -11100mV,检测限为0.04 g.ml,定量限制为0.1g。估计ml。

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