The molecular mechanisms of interactions between bioactive peptides and angiotensin-converting enzyme

Bioorganic and Medicinal Chemistry Letters

Volumn 21, Issue 13, 2011, Pages 3898-3904

  Pan, Daodong ^a,b   Guo, Huiqing ^b   Zhao, Bo ^b   Cao, Jinxuan ^a  

^a NINGBO UNIVERSITY   (China)

^b NANJING NORMAL UNIVERSITY   (China)

Author keywords

ACE inhibition; Elucidate; Milk protein peptides; Molecular mechanisms

Indexed keywords

ANTIHYPERTENSIVE AGENT; DIPEPTIDYL CARBOXYPEPTIDASE; GLYCYLLYSYLPROLINE; ISOLEUCYLPROLYLALANINE; MILK PROTEIN; PEPTIDE DERIVATIVE; PHENYLALANYLPROLINE; UNCLASSIFIED DRUG; ZINC ION;

AMINO TERMINAL SEQUENCE; ANTIHYPERTENSIVE ACTIVITY; ARTICLE; BINDING KINETICS; CARBOXY TERMINAL SEQUENCE; CATALYSIS; COMPETITIVE INHIBITION; CRYSTAL STRUCTURE; DRUG STRUCTURE; ENZYME ACTIVE SITE; HYDROGEN BOND; HYDROPHILICITY; HYDROPHOBICITY; IN VITRO STUDY; MOLECULAR DOCKING; MOLECULAR INTERACTION; PROTEIN PROTEIN INTERACTION; STATIC ELECTRICITY; X RAY CRYSTALLOGRAPHY;

ANGIOTENSIN-CONVERTING ENZYME INHIBITORS; BINDING SITES; ENZYME ACTIVATION; ENZYME INHIBITORS; HUMANS; HYDROGEN BONDING; MILK PROTEINS; MODELS, MOLECULAR; MOLECULAR STRUCTURE; PEPTIDES; ZINC;

EID: 79958752694     PISSN: 0960894X     EISSN: 14643405     Source Type: Journal    
DOI: 10.1016/j.bmcl.2011.05.033     Document Type: Article

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