Alpha-amylase (α-amylase) not long ago has acquire recognition as a possible drug target for the management of diabetes. Here, we have investigated the binding and enzyme activity of α-amylase by hesperidin; a naturally occurring flavanone having wide therapeutic potential. Hesperidin exerted an inhibitory influence on α-amylase activity with an IC₅₀ value of 16.6 µM. Hesperidin shows a significant binding toward α-amylase with a binding constant (K_a) of the order of 10⁴ M⁻¹. The evaluation of thermodynamic parameters (∆H and ∆S) suggested that van der Waals force and hydrogen bonding drive seemingly specific hesperidin-α-amylase complex formation. Glycation and oxidation studies were performed using human serum albumin (HSA) as ideal protein. Hesperidin inhibited fructosamine content ≈40% at 50 µM and inhibited advanced glycation end products (AGEs) formation by 71.2% at the same concentration. Moreover, significant recovery was evident in free –SH groups and carbonyl content of HSA. Additionally, molecular docking also entrenched in vitro observations and provided an insight into the important residues (Trp58, Gln63, His101, Glu233, Asp300, and His305) at the heart of hesperidin-α-amylase interaction. This study delineates mechanistic insight of hesperidin-α-amylase interaction and provides a platform for use of hesperidin to treat AGEs directed diseases.

不久前，α-淀粉酶（α-amylase）已被认为是治疗糖尿病的可能药物靶点。在这里，我们研究了橙皮苷对 α-淀粉酶的结合和酶活性；一种天然存在的黄烷酮，具有广泛的治疗潜力。橙皮苷对 α-淀粉酶活性具有抑制作用，IC ₅₀值为 16.6 µM。橙皮苷显示出与α-淀粉酶的显着结合_，结合常数( Ka )约为10 ⁴ M ^-1 。热力学参数（Δ H和 Δ S ）的评估表明，范德华力和氢键驱动看似特定的橙皮苷-α-淀粉酶复合物的形成。使用人血清白蛋白（HSA）作为理想蛋白质进行糖化和氧化研究。橙皮苷在 50 µM 时可抑制果糖胺含量约 40%，在相同浓度下可抑制晚期糖基化终末产物 (AGE) 的形成 71.2%。此外，游离-SH基团和HSA的羰基含量也有明显的恢复。此外，分子对接还巩固了体外观察，并提供了对橙皮苷-α-淀粉酶相互作用核心的重要残基（Trp58、Gln63、His101、Glu233、Asp300 和 His305）的深入了解。这项研究描绘了橙皮苷-α-淀粉酶相互作用的机制，并为使用橙皮苷治疗 AGE 相关疾病提供了一个平台。