Investigation of Potential cGMP-Specific PDE V and Aminopeptidase N Inhibitors of <i>Allium ampeloprasum</i> L. and Its Bioactive Components: Kinetic and Molecular Docking Studies
The primary objectives of this study were to assess the inhibitory effects of <i>Allium ampeloprasum</i> L. extract (AAE) and its derived organosulfur and polyphenolic compounds on the enzymatic activities of cGMP-specific PDE V (PDE5) and aminopeptidase N (APN). Additionally, the study...
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MDPI AG
2023-08-01
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Online Access: | https://www.mdpi.com/1422-0067/24/17/13319 |
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author | Jun-Hui Choi Seung-Man Park Seung Kim |
author_facet | Jun-Hui Choi Seung-Man Park Seung Kim |
author_sort | Jun-Hui Choi |
collection | DOAJ |
description | The primary objectives of this study were to assess the inhibitory effects of <i>Allium ampeloprasum</i> L. extract (AAE) and its derived organosulfur and polyphenolic compounds on the enzymatic activities of cGMP-specific PDE V (PDE5) and aminopeptidase N (APN). Additionally, the study aimed to investigate their potential as inhibitors against these two target enzymes through kinetic analyses and molecular docking studies. The in vitro enzyme assays demonstrated that both AAE and its derived compounds significantly decreased the activity of PDE5 and APN. Further analyses involving kinetics and molecular docking provided insights into the specific inhibitor types of AAE and its derived compounds along with the proposed molecular docking models illustrating the interactions between the ligands (the compounds) and the enzymes (PDE5 and APN). In particular, AAE-derived polyphenolic compounds showed relatively stable binding affinity (−7.2 to −8.3 kcal/mol) on PDE5 and APN. Our findings proved the potential as an inhibitor against PDE5 and APN of AAE and AAE-derived organosulfur and polyphenolic compounds as well as a functional material for erectile dysfunction improvement. |
first_indexed | 2024-03-10T23:21:12Z |
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issn | 1661-6596 1422-0067 |
language | English |
last_indexed | 2024-03-10T23:21:12Z |
publishDate | 2023-08-01 |
publisher | MDPI AG |
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series | International Journal of Molecular Sciences |
spelling | doaj.art-25d75a86328d4684b2a295a02029615f2023-11-19T08:15:37ZengMDPI AGInternational Journal of Molecular Sciences1661-65961422-00672023-08-0124171331910.3390/ijms241713319Investigation of Potential cGMP-Specific PDE V and Aminopeptidase N Inhibitors of <i>Allium ampeloprasum</i> L. and Its Bioactive Components: Kinetic and Molecular Docking StudiesJun-Hui Choi0Seung-Man Park1Seung Kim2Department of Health Functional Food, Gwangju University, Gwangju 61743, Republic of KoreaHyundai F&B Co., Ltd., Gwangju 61200, Republic of KoreaDepartment of Health Functional Food, Gwangju University, Gwangju 61743, Republic of KoreaThe primary objectives of this study were to assess the inhibitory effects of <i>Allium ampeloprasum</i> L. extract (AAE) and its derived organosulfur and polyphenolic compounds on the enzymatic activities of cGMP-specific PDE V (PDE5) and aminopeptidase N (APN). Additionally, the study aimed to investigate their potential as inhibitors against these two target enzymes through kinetic analyses and molecular docking studies. The in vitro enzyme assays demonstrated that both AAE and its derived compounds significantly decreased the activity of PDE5 and APN. Further analyses involving kinetics and molecular docking provided insights into the specific inhibitor types of AAE and its derived compounds along with the proposed molecular docking models illustrating the interactions between the ligands (the compounds) and the enzymes (PDE5 and APN). In particular, AAE-derived polyphenolic compounds showed relatively stable binding affinity (−7.2 to −8.3 kcal/mol) on PDE5 and APN. Our findings proved the potential as an inhibitor against PDE5 and APN of AAE and AAE-derived organosulfur and polyphenolic compounds as well as a functional material for erectile dysfunction improvement.https://www.mdpi.com/1422-0067/24/17/13319<i>Allium ampeloprasum</i> L.aminopeptidase NcGMP-specific PDE Vkineticsmolecular docking |
spellingShingle | Jun-Hui Choi Seung-Man Park Seung Kim Investigation of Potential cGMP-Specific PDE V and Aminopeptidase N Inhibitors of <i>Allium ampeloprasum</i> L. and Its Bioactive Components: Kinetic and Molecular Docking Studies International Journal of Molecular Sciences <i>Allium ampeloprasum</i> L. aminopeptidase N cGMP-specific PDE V kinetics molecular docking |
title | Investigation of Potential cGMP-Specific PDE V and Aminopeptidase N Inhibitors of <i>Allium ampeloprasum</i> L. and Its Bioactive Components: Kinetic and Molecular Docking Studies |
title_full | Investigation of Potential cGMP-Specific PDE V and Aminopeptidase N Inhibitors of <i>Allium ampeloprasum</i> L. and Its Bioactive Components: Kinetic and Molecular Docking Studies |
title_fullStr | Investigation of Potential cGMP-Specific PDE V and Aminopeptidase N Inhibitors of <i>Allium ampeloprasum</i> L. and Its Bioactive Components: Kinetic and Molecular Docking Studies |
title_full_unstemmed | Investigation of Potential cGMP-Specific PDE V and Aminopeptidase N Inhibitors of <i>Allium ampeloprasum</i> L. and Its Bioactive Components: Kinetic and Molecular Docking Studies |
title_short | Investigation of Potential cGMP-Specific PDE V and Aminopeptidase N Inhibitors of <i>Allium ampeloprasum</i> L. and Its Bioactive Components: Kinetic and Molecular Docking Studies |
title_sort | investigation of potential cgmp specific pde v and aminopeptidase n inhibitors of i allium ampeloprasum i l and its bioactive components kinetic and molecular docking studies |
topic | <i>Allium ampeloprasum</i> L. aminopeptidase N cGMP-specific PDE V kinetics molecular docking |
url | https://www.mdpi.com/1422-0067/24/17/13319 |
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