Investigation of the Interaction Between Angiotensin-Converting Enzyme (ACE) and ACE-Inhibitory Tripeptide from Casein
Cuicui Yang, Tianzhao Xie, Mengmeng Cai, Xiaoting Xu, Muzijun Li, Pengru Liu, Xiongdiao Lan, Anastasios Lymperopoulos, Guan-Jhong Huang · 2024
Read Investigation of the Interaction Between Angiotensin-Converting Enzyme (ACE) and ACE-Inhibitory Tripeptide from Casein by Cuicui Yang, Tianzhao Xie, Mengmeng Cai, Xiaoting Xu, Muzijun Li, Pengru Liu, Xiongdiao Lan, Anastasios Lymperopoulos, Guan-Jhong Huang (2024) in the Tower of Babel, a free online library of public-domain works preserved in clean, searchable text. No sign-up. The full text is served as a plain-text file at a predictable URL, where text is present: https://antarctic-labs.com/tower-of-babel/pmc-11641789.txt.
Description
Cuicui Yang and colleagues dissect how a milk-derived peptide blocks a blood pressure enzyme, in a study published in two thousand twenty-four. The enzyme is ACE, target of many hypertension drugs. Food-derived inhibitors could offer gentler alternatives or leads.
The peptide, three amino acids long and called LLY, came from casein hydrolysate. It inhibited ACE strongly and stayed stable. Kinetic plots showed it binds away from the enzyme's active site, a non-competitive pattern. Molecular docking agreed with that reading. Spectroscopy and atomic force microscopy watched the enzyme change shape on binding. The systematic interaction map matters for designing peptide-based antihypertensives that survive digestion and reach their target.
Catalog record
| CREATOR | Cuicui Yang, Tianzhao Xie, Mengmeng Cai, Xiaoting Xu, Muzijun Li, Pengru Liu, Xiongdiao Lan, Anastasios Lymperopoulos, Guan-Jhong Huang |
|---|---|
| YEAR | 2024 |
| COLLECTION | PAPERS |
| FORMAT | TXT |
| FILE SIZE | 42 KB |
| VERSION | 1.0 |
| LICENSE | CC BY 4.0 |
| RIGHTS | CC BY |
| SOURCE | Europe PMC |