School of Chemistry and Chemical Engineering , Guangxi University for Nationalities , Nanning , Guangxi 530008 , People's Republic of China.
Institute of Chemical Sciences , University of Peshawar , Peshawar , Khyber Pakhtunkhwa 25120 , Pakistan.
J Agric Food Chem. 2018 Dec 26;66(51):13414-13422. doi: 10.1021/acs.jafc.8b04303. Epub 2018 Dec 13.
Angiotensin-converting enzyme (ACE) inhibitory peptides derived from food protein exhibited antihypertensive effects by inhibiting ACE activity. In this work, the interaction between ACE inhibitory peptide GMKCAF (GF-6) and ACE was studied by isothermal titration calorimetry (ITC), molecular docking, ultraviolet absorption spectroscopy, fluorescence spectroscopy, and circular dichroism spectroscopy. Experimental results revealed that the binding of GF-6 to ACE was a spontaneous exothermic process driven by both enthalpy and entropy. The interaction occurred via a static quenching mechanism and involved the alteration of the conformation of ACE. In addition, ITC and molecular docking results indicated binding of GF-6 to ACE via multiple binding sites on the protein surface. This study could be deemed helpful for the better understanding of the inhibitory mechanism of ACE inhibitory peptides.
血管紧张素转化酶（ACE）抑制肽来源于食物蛋白，通过抑制 ACE 活性发挥降血压作用。在这项工作中，通过等温滴定量热法（ITC）、分子对接、紫外吸收光谱、荧光光谱和圆二色光谱研究了 ACE 抑制肽 GMKCAF（GF-6）与 ACE 的相互作用。实验结果表明，GF-6 与 ACE 的结合是一个自发的、由焓和熵驱动的放热过程。这种相互作用是通过静态猝灭机制发生的，涉及 ACE 构象的改变。此外，ITC 和分子对接结果表明，GF-6 通过 ACE 表面的多个结合位点与 ACE 结合。这项研究有助于更好地理解 ACE 抑制肽的抑制机制。
