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首页> 外文期刊>RSC Advances >Spectroscopic characterization of the warfarin drug-binding site of folded and unfolded human serum albumin anchored on gold nanoparticles: effect of bioconjugation on the loading capacity
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Spectroscopic characterization of the warfarin drug-binding site of folded and unfolded human serum albumin anchored on gold nanoparticles: effect of bioconjugation on the loading capacity

机译：固定在金纳米颗粒上的折叠和未折叠人类血清白蛋白的华法林药物结合位点的光谱表征：生物共轭对负载能力的影响

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Protein-conjugated gold nanoparticles (AuNPs) have recently shown promising applications in medicine, owing to their inertness and biocompatibility. Herein, we studied the spectroscopy of 25?nm diameter AuNPs, coated with human serum albumin (HSA) as a model drug carrier. The morphology and coating of the AuNPs were examined using transmission electron microscopy and dynamic light scattering. Resonance energy transfer from the sole tryptophan of HSA (Trp214) to the AuNPs indicates a single layer of protein coverage. Using fluorescein (FL) to probe the warfarin drug-binding site in HSA revealed an increase in the HSA–FL binding by ～4.5 times when HSA is anchored on the nanoparticle surface, indicating a rise in the loading capacity. Femtosecond transient absorption measurements of the surface plasmonic resonance band of the AuNPs show three ultrafast dynamics that are involved in the relaxation process. The three decay components were assigned to the electron–electron (～400 fs), electron–phonon (～2.0 ps) and phonon–phonon (200–250 ps) interactions. These dynamics were not changed upon coating the AuNPs with HSA which indicates the chemical and physical stability of the AuNPs upon bioconjugation. Chemical unfolding of the warfarin binding site with guanidine hydrochloride (GdnHCl) was studied by measuring the spectral shift in the Trp214 fluorescence and the appearance of the Tyr fluorescence. Unfolding was shown to start at [GdnHCl] ≥ 2.0 M and is complete at [GdnHCl] = 6.0 M. HSA anchored onto the nanoparticle surface shows more resistance to the unfolding effect which is attributed to the stability of the native form of HSA on the nanoparticle surface. On the other hand, upon complete unfolding, a larger red shift in the Trp214 fluorescence was observed for the HSA–AuNP complex. This observation indicates that, upon unfolding, the HSA molecule is still anchored on the AuNP surface in which subdomain IIA is facing the outer water molecules in the bulk solution as well as the hydration shell rather than the core of the nanoparticle. The current study is important for a better understanding of the physical and dynamical properties of protein-coated metal nanoparticles, which is expected to help in optimizing their properties for critical applications in nanomedicine.
机译：蛋白质缀合的金纳米颗粒（AuNPs）由于其惰性和生物相容性，最近在医学上显示出有希望的应用。在这里，我们研究了直径25？nm的AuNPs的光谱，该纳米金涂有人血清白蛋白（HSA）作为模型药物载体。使用透射电子显微镜和动态光散射检查了AuNPs的形态和涂层。从HSA的唯一色氨酸（Trp214）到AuNPs的共振能量转移表明单层蛋白质覆盖。用荧光素（FL）探测HSA中的华法林药物结合位点显示，当HSA锚定在纳米颗粒表面时，HSA-FL结合增加了约4.5倍，表明负载量增加了。飞秒的AuNPs表面等离子体共振带的瞬态吸收测量结果表明，弛豫过程涉及三个超快速动力学。这三个衰减分量分别分配给电子-电子（〜400 fs），电子－声子（〜2.0 ps）和声子－声子（200〜250 ps）相互作用。当用HSA包被AuNP时，这些动力学没有改变，这表明在生物缀合后AuNP的化学和物理稳定性。通过测量Trp214荧光的光谱位移和Tyr荧光的外观研究了华法林与盐酸胍（GdnHCl）结合位点的化学解折叠。展开显示在[GdnHCl]≥2.0 M时开始，并在[GdnHCl] = 6.0 M时完成。锚定在纳米颗粒表面上的HSA显示出对展开效果的更大抵抗力，这归因于天然形式的HSA在表面上的稳定性。纳米颗粒表面。另一方面，完全展开后，HSA–AuNP复合物在Trp214荧光中观察到较大的红移。该观察结果表明，在展开时，HSA分子仍锚定在AuNP表面上，其中亚结构域IIA面向本体溶液中的外部水分子以及水合壳而不是纳米颗粒的核心。当前的研究对于更好地了解蛋白包被的金属纳米颗粒的物理和动力学性质很重要，这有望帮助优化其性质以用于纳米药物的关键应用。

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