| Article ID | Journal | Published Year | Pages | File Type |
|---|---|---|---|---|
| 1372924 | Bioorganic & Medicinal Chemistry Letters | 2011 | 7 Pages |
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+. 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 the interaction with Zn2+. The interactions, including H-bonds, hydrophobic, hydrophilic, and electrostatic interactions, as well as the interaction with Zn2+, were responsible for the binding between the bioactive peptides and ACE.
Graphical abstractThis work elucidates the modes and molecular mechanisms of the interaction of Ile-Pro-Ala (IPA), Phe-Pro (FP) and Gly-Lys-Pro (GKP) with inhibit angiotensin I-converting enzyme (ACE), a protein with very important roles in blood-pressure regulation.Figure optionsDownload full-size imageDownload as PowerPoint slide
