Mechanistic Insights into Angiotensin I-Converting Enzyme Inhibitory Tripeptides to Decipher the Chemical Basis of Their Activity.
angiotensin I-converting enzyme
antihypertensive peptides
bioactive peptides
structure−activity relationship
Journal
Journal of agricultural and food chemistry
ISSN: 1520-5118
Titre abrégé: J Agric Food Chem
Pays: United States
ID NLM: 0374755
Informations de publication
Date de publication:
21 Sep 2022
21 Sep 2022
Historique:
pubmed:
9
9
2022
medline:
24
9
2022
entrez:
8
9
2022
Statut:
ppublish
Résumé
Food proteins are an important source of bioactive peptides, and the angiotensin I-converting enzyme (ACE) inhibitors are worthy of attention for their possible beneficial effects in subjects with mild hypertension. However, the chemical basis underpinning their activity is not well-understood, hampering the discovery of novel inhibitory sequences from the plethora of peptides encrypted in food proteins. This work combined computational and
Identifiants
pubmed: 36074807
doi: 10.1021/acs.jafc.2c04755
pmc: PMC9501895
doi:
Substances chimiques
Angiotensin-Converting Enzyme Inhibitors
0
Peptides
0
Peptidyl-Dipeptidase A
EC 3.4.15.1
Types de publication
Journal Article
Langues
eng
Sous-ensembles de citation
IM
Pagination
11572-11578Références
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