Angiotensin converting enzyme (ACE)-peptide interactions: Inhibition kinetics, in silico molecular docking and stability study of three novel peptides generated from palm kernel cake proteins

Angiotensin converting enzyme (ACE)-peptide interactions: Inhibition kinetics, in silico molecular docking and stability study of three novel peptides generated from palm kernel cake proteins

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Three novel peptide sequences identified from palm kernel cake (PKC) generated protein hydrolysate including YLLLK, WAFS and GVQEGAGHYALL were used for stability study against angiotensin-converting enzyme (ACE), ACE-inhibition kinetics and molecular docking studies. Results showed that the peptides...

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Bibliographic Details
Main Authors: Abidin, N.B.Z (Author), Auwal, S.M (Author), Chay, S.Y (Author), Haiyee, Z.A (Author), Saari, N. (Author), Sikin, A.M (Author), Zarei, M. (Author)
Format: Article
Language:English
Published: MDPI AG 2019
Subjects:
ACE protein, human
amino acid sequence
Angiotensin converting enzyme inhibitory activity
animal
Animals
Article
binding affinity
carboxy terminal sequence
catalysis
Catalysis
Catalytic Domain
catalytic efficiency
chemistry
computer model
controlled study
dipeptidyl carboxypeptidase
drug effect
enzyme active site
enzyme inhibition
enzyme mechanism
enzyme stability
enzyme substrate complex
gene expression regulation
Gene Expression Regulation
gvqegaghyall protein
high performance liquid chromatography
human
Humans
hydrogen bond
hydrolysis
Hydrolysis
IC50
incubation time
inhibition constant
inhibition kinetics
kinetics
Kinetics
metabolism
Michaelis constant
Models, Molecular
molecular docking
Molecular docking
Molecular Docking Simulation
molecular model
palm kernel cake protein
palm oil
Palm Oil
papain
Peptide
peptide fragment
Peptide Fragments
Peptidyl-Dipeptidase A
plant protein
Plant Proteins
protein cleavage
protein degradation
protein hydrolysate
reversed phase high performance liquid chromatography
static electricity
unclassified drug
wafs protein
ylllk protein
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