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Size-responsive differential modulation in α-amylase by MPA-CdSe QDs: multispectroscopy and molecular docking study
Journal of Nanoparticle Research ( IF 2.5 ) Pub Date : 2021-08-21 , DOI: 10.1007/s11051-021-05298-y
Jagriti Gupta 1 , Paulraj Rajamani 1 , Kishan Das 2
Affiliation  

QDs has been deftly explored, studied, and optimized because of its unique optical and physicochemical properties. However, their high production and usage arouses the concern of accidental or unavoidable release in environment which can have toxic impact on animals. It is thus indispensable to comprehend its non-target effect. In the present study, interaction of vital digestive enzyme α-amylase was investigated with water-soluble mercaptopropionic acid (MPA)-capped CdSe QDs of five different sizes (1.9 nm, 2.3 nm, 2.5 nm, 3.3 nm, and 3.9 nm) by various spectroscopic techniques. Distinctive increase in absorption spectra and fluorescence quenching of α-amylase was observed chiefly due to α-amylase-CdSe QDs ground state complex formation. Binding constant (Kb), binding sites (n), and quenching constant (Ksv) were also determined. The results illustrated that binding of α-amylase with CdSe QDs followed 1:1 stoichiometry and induced conformational changes in dose- and size-dependent manner. Effect on α-amylase activity in complex form with size varied CdSe QDs suggested higher inhibition of enzymatic activity by smaller size QDs as compared to larger size. Molecular docking of MPA ligand with α-amylase revealed that interaction was majorly driven by hydrophobic forces. It further suggested that MPA did not interact with active site of α-amylase, thus acting as non-competitive inhibitor. The study thus involved a comprehensive analysis of the structural and functional modulation in α-amylase by interaction with hydrophilic MPA-capped CdSe QDs of different sizes.

Graphical abstract



中文翻译:

MPA-CdSe QD 对 α-淀粉酶的大小响应差异调节:多光谱和分子对接研究

量子点因其独特的光学和物理化学性质而被巧妙地探索、研究和优化。然而,它们的高产量和使用量引起了人们对环境中意外或不可避免的释放可能对动物产生毒性影响的担忧。因此,理解其非目标效应是必不可少的。在本研究中,研究了重要消化酶 α-淀粉酶与五种不同尺寸(1.9 nm、2.3 nm、2.5 nm、3.3 nm 和 3.9 nm)的水溶性巯基丙酸 (MPA) 封端的 CdSe QD 的相互作用。各种光谱技术。观察到 α-淀粉酶的吸收光谱和荧光猝灭的显着增加主要是由于 α-淀粉酶-CdSe QDs 基态复合物的形成。结合常数 (K b )、结合位点 (n) 和淬灭常数 (Ksv ) 也被确定。结果表明,α-淀粉酶与 CdSe QD 的结合遵循 1:1 的化学计量,并以剂量​​和大小依赖性方式诱导构象变化。大小不同的 CdSe QD 对复合形式的 α-淀粉酶活性的影响表明,与较大尺寸的 QD 相比,较小尺寸的 QD 对酶活性的抑制更高。MPA 配体与 α-淀粉酶的分子对接表明相互作用主要由疏水力驱动。这进一步表明 MPA 不与 α-淀粉酶的活性位点相互作用,从而起到非竞争性抑制剂的作用。因此,该研究涉及通过与不同大小的亲水性 MPA 加帽 CdSe QD 相互作用对 α-淀粉酶的结构和功能调节进行综合分析。

图形摘要

更新日期:2021-08-23
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