School of Biotechnology, Institute of Science, Banaras Hindu University, Varanasi 221005, India.
School of Biotechnology, Institute of Science, Banaras Hindu University, Varanasi 221005, India.
Spectrochim Acta A Mol Biomol Spectrosc. 2024 Jun 5;314:124160. doi: 10.1016/j.saa.2024.124160. Epub 2024 Mar 16.
This study looked at the effects of acarbose (ACA) and quercetin (QUE) on α-amylase activity, employing QUE and ACA to measure enzyme activity. The study observed that both drugs suppressed α-amylase activity, with greater inhibition reported at higher concentrations. The use of tryptophan residues as an intrinsic fluorescence probe permitted the observation of conformational changes in α-amylase, with CD measurements utilized to explore the secondary structure in the presence of QUE and ACA. Docking studies revealed an effective interaction between α-amylase, quercetin and acarbose, with a higher binding energy. Finally, a trajectory analysis was done to establish the stability and volatility of these complexes. These findings have potential significance for the development of new α-amylase-related therapeutics.
本研究考察了阿卡波糖（ACA）和槲皮素（QUE）对α-淀粉酶活性的影响，采用 QUE 和 ACA 来测定酶活性。研究观察到这两种药物都抑制了α-淀粉酶的活性，并且在较高浓度下报告了更大的抑制作用。使用色氨酸残基作为内在荧光探针，允许观察α-淀粉酶的构象变化，利用 CD 测量来研究 QUE 和 ACA 存在下的二级结构。对接研究表明，α-淀粉酶、槲皮素和阿卡波糖之间存在有效的相互作用，具有更高的结合能。最后，进行了轨迹分析以确定这些复合物的稳定性和挥发性。这些发现对于开发新的与α-淀粉酶相关的治疗方法具有潜在的意义。
