The molecular mechanisms of interactions between bioactive peptides and angiotensin-converting enzyme
The ability of milk-protein derived Ile-Pro-Ala (IPA), Phe-Pro (FP) and Gly-Lys-Pro (GKP) peptides to inhibit angiotensin I-converting enzyme (ACE), a protein with an important role in blood-pressure regulation, were verified in vitro and in vivo. This work elucidates the modes and molecular mechanisms of the interaction of IPA, FP and GKP with ACE, including mechanisms that bind the peptides to the cofactor Zn2+, using the ACCELRYS Discovery Studio2.1 software. It was observed that the best docking poses obtained for IPA, FP and GKP were at the ACE catalytic site with very similar modes of interaction, including coordination with Zn2+. The interactions, including H-bonds, hydrophobic, hydrophilic, and electrostatic interactions, as well as the coordination with Zn2+, were responsible for the binding between the bioactive peptides and ACE.
Huiqing Guo Hui Mao Bo Zhao Daodong Pan
Jiangsu Key Laboratory of Biofunctional Materials, College of Chemistry and Material Science, Nanjin Jiangsu Key Laboratory of Biofunctional Materials, College of Chemistry and Material Science, Nanjin
国际会议
武汉
英文
497-511
2010-09-01（万方平台首次上网日期，不代表论文的发表时间）