Title : Study on the domain selective inhibition of angiotensin-converting enzyme (ACE) by food-derived tyrosine-containing dipeptides.

Pub. Date : 2021 Jul

PMID : 34060658






5 Functional Relationships(s)
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1 Study on the domain selective inhibition of angiotensin-converting enzyme (ACE) by food-derived tyrosine-containing dipeptides. Dipeptides angiotensin I converting enzyme Homo sapiens
2 Study on the domain selective inhibition of angiotensin-converting enzyme (ACE) by food-derived tyrosine-containing dipeptides. Dipeptides angiotensin I converting enzyme Homo sapiens
3 In this article, the selective inhibition of several tyrosine-containing dipeptides on N and C domain of ACE (angiotensin-converting enzyme) was studied, and the interaction mode of ACE and inhibitors was simulated by molecular docking. Dipeptides angiotensin I converting enzyme Homo sapiens
4 In this article, the selective inhibition of several tyrosine-containing dipeptides on N and C domain of ACE (angiotensin-converting enzyme) was studied, and the interaction mode of ACE and inhibitors was simulated by molecular docking. Dipeptides angiotensin I converting enzyme Homo sapiens
5 The results showed that the food-derived dipeptides AY (Ala-Tyr), LY (Leu-Tyr), and IY (Ile-Tyr) containing tyrosine at the C-terminal were favorable structures for selective inhibition of ACE C-domain. Dipeptides angiotensin I converting enzyme Homo sapiens