Arachin derived peptides as selective angiotensin I-converting enzyme (ACE) inhibitors: Structure-activity relationship

Peptides

Volumn 31, Issue 6, 2010, Pages 1165-1176

  Jimsheena, V K ^a   Gowda, Lalitha R ^a  

^a CENTRAL FOOD TECHNOLOGICAL RESEARCH INSTITUTE   (India)

Author keywords

Arachis hypogaea; Bioactive peptides; Hypertension; Molecular docking; Protease P; Tripeptide inhibitors

Indexed keywords

DIPEPTIDYL CARBOXYPEPTIDASE; DIPEPTIDYL CARBOXYPEPTIDASE INHIBITOR; ISOLEUCYLGLUTAMYLPROLINE; ISOLEUCYLGLUTAMYLTRYPTOPHAN; ISOLEUCYLGLUTAMYLTYROSINE; ISOLEUCYLLYSYLPROLINE; ISOLEUCYLLYSYLTRYPTOPHAN; ISOLEUCYLLYSYLTYROSINE; ISOLEUCYLPROLYLPROLINE; LISINOPRIL; PEPTIDE DERIVATIVE; TRIPEPTIDE; UNCLASSIFIED DRUG; VALYLPROLYLPROLINE; ZINC ION;

AMINO TERMINAL SEQUENCE; ARTICLE; BLOOD PRESSURE REGULATION; CATALYSIS; CONTROLLED STUDY; DRUG ISOLATION; ENZYME ACTIVE SITE; IC 50; NONHUMAN; PRIORITY JOURNAL; STRUCTURE ACTIVITY RELATION;

ANGIOTENSIN-CONVERTING ENZYME INHIBITORS; ANTIHYPERTENSIVE AGENTS; LISINOPRIL; MODELS, MOLECULAR; OLIGOPEPTIDES; PEPTIDYL-DIPEPTIDASE A; PLANT PROTEINS; STRUCTURE-ACTIVITY RELATIONSHIP;

ARACHIS HYPOGAEA;

EID: 77952100977     PISSN: 01969781     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.peptides.2010.02.022     Document Type: Article

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