Identification of a novel ACE-inhibitory peptide from casein and evaluation of the inhibitory mechanisms

Maolin Tu; Cong Wang; Cheng Chen; Ruyi Zhang; Hanxiong Liu; Weihong Lu; Lianzhou Jiang; Ming Du

doi:10.1016/j.foodchem.2018.02.107

Identification of a novel ACE-inhibitory peptide from casein and evaluation of the inhibitory mechanisms

Maolin Tu
, Cong Wang
, Cheng Chen
, Ruyi Zhang
, Hanxiong Liu
, Weihong Lu
, Lianzhou Jiang
, Ming Du^*

^*Corresponding author for this work

Dalian Polytechnic University
School of Chemistry and Chemical Engineering, Harbin Institute of Technology
Northeast Agricultural University

Research output: Contribution to journal › Article › peer-review

200 Scopus citations

Abstract

Various bioactive peptides are continuously being identified from casein hydrolysates. In this work, a novel angiotensin I-converting enzyme (ACE)-inhibitory (ACEI) peptide, NMAINPSKENLCSTFCK, derived from the α_s2-casein fragment residues 25–41, was screened and identified by UPLC-ESI-Q-TOF-MS/MS from tryptic casein hydrolysate. The IC₅₀ value of the peptide, determined by an HPLC method, was 129.07 μM. The Lineweaver-Burk plot showed that this peptide acted as a mixed-type inhibitor against ACE, which might be attributed to the peptide being susceptible to degradation by ACE, indicating that the mixed-type inhibition could partly be a result of newly generated peptide fragments. The physicochemical characteristics and the secondary structure were evaluated by circular dichroism analysis and online prediction software (Expasy, PepDraw, and ProtParam) to identify the basic characteristics of this peptide. Moreover, molecular docking was simulated by Discovery Studio 2017 R2 software to provide the potential mechanisms underlying the ACEI activity of the peptides.

Original language	English
Pages (from-to)	98-104
Number of pages	7
Journal	Food Chemistry
Volume	256
DOIs	https://doi.org/10.1016/j.foodchem.2018.02.107
State	Published - 1 Aug 2018
Externally published	Yes

Keywords

ACE-inhibitory activity
Casein peptide
Identification
Molecular docking
UPLC-ESI-Q-TOF-MS/MS

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10.1016/j.foodchem.2018.02.107

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title = "Identification of a novel ACE-inhibitory peptide from casein and evaluation of the inhibitory mechanisms",

abstract = "Various bioactive peptides are continuously being identified from casein hydrolysates. In this work, a novel angiotensin I-converting enzyme (ACE)-inhibitory (ACEI) peptide, NMAINPSKENLCSTFCK, derived from the αs2-casein fragment residues 25–41, was screened and identified by UPLC-ESI-Q-TOF-MS/MS from tryptic casein hydrolysate. The IC50 value of the peptide, determined by an HPLC method, was 129.07 μM. The Lineweaver-Burk plot showed that this peptide acted as a mixed-type inhibitor against ACE, which might be attributed to the peptide being susceptible to degradation by ACE, indicating that the mixed-type inhibition could partly be a result of newly generated peptide fragments. The physicochemical characteristics and the secondary structure were evaluated by circular dichroism analysis and online prediction software (Expasy, PepDraw, and ProtParam) to identify the basic characteristics of this peptide. Moreover, molecular docking was simulated by Discovery Studio 2017 R2 software to provide the potential mechanisms underlying the ACEI activity of the peptides.",

keywords = "ACE-inhibitory activity, Casein peptide, Identification, Molecular docking, UPLC-ESI-Q-TOF-MS/MS",

author = "Maolin Tu and Cong Wang and Cheng Chen and Ruyi Zhang and Hanxiong Liu and Weihong Lu and Lianzhou Jiang and Ming Du",

note = "Publisher Copyright: {\textcopyright} 2018 Elsevier Ltd",

year = "2018",

month = aug,

day = "1",

doi = "10.1016/j.foodchem.2018.02.107",

language = "英语",

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AU - Tu, Maolin

AU - Wang, Cong

AU - Chen, Cheng

AU - Zhang, Ruyi

AU - Liu, Hanxiong

AU - Lu, Weihong

AU - Jiang, Lianzhou

AU - Du, Ming

PY - 2018/8/1

Y1 - 2018/8/1

N2 - Various bioactive peptides are continuously being identified from casein hydrolysates. In this work, a novel angiotensin I-converting enzyme (ACE)-inhibitory (ACEI) peptide, NMAINPSKENLCSTFCK, derived from the αs2-casein fragment residues 25–41, was screened and identified by UPLC-ESI-Q-TOF-MS/MS from tryptic casein hydrolysate. The IC50 value of the peptide, determined by an HPLC method, was 129.07 μM. The Lineweaver-Burk plot showed that this peptide acted as a mixed-type inhibitor against ACE, which might be attributed to the peptide being susceptible to degradation by ACE, indicating that the mixed-type inhibition could partly be a result of newly generated peptide fragments. The physicochemical characteristics and the secondary structure were evaluated by circular dichroism analysis and online prediction software (Expasy, PepDraw, and ProtParam) to identify the basic characteristics of this peptide. Moreover, molecular docking was simulated by Discovery Studio 2017 R2 software to provide the potential mechanisms underlying the ACEI activity of the peptides.

AB - Various bioactive peptides are continuously being identified from casein hydrolysates. In this work, a novel angiotensin I-converting enzyme (ACE)-inhibitory (ACEI) peptide, NMAINPSKENLCSTFCK, derived from the αs2-casein fragment residues 25–41, was screened and identified by UPLC-ESI-Q-TOF-MS/MS from tryptic casein hydrolysate. The IC50 value of the peptide, determined by an HPLC method, was 129.07 μM. The Lineweaver-Burk plot showed that this peptide acted as a mixed-type inhibitor against ACE, which might be attributed to the peptide being susceptible to degradation by ACE, indicating that the mixed-type inhibition could partly be a result of newly generated peptide fragments. The physicochemical characteristics and the secondary structure were evaluated by circular dichroism analysis and online prediction software (Expasy, PepDraw, and ProtParam) to identify the basic characteristics of this peptide. Moreover, molecular docking was simulated by Discovery Studio 2017 R2 software to provide the potential mechanisms underlying the ACEI activity of the peptides.

KW - ACE-inhibitory activity

KW - Casein peptide

KW - Identification

KW - Molecular docking

KW - UPLC-ESI-Q-TOF-MS/MS

UR - https://www.scopus.com/pages/publications/85042430150

U2 - 10.1016/j.foodchem.2018.02.107

DO - 10.1016/j.foodchem.2018.02.107

M3 - 文章

C2 - 29606478

AN - SCOPUS:85042430150

SN - 0308-8146

VL - 256

SP - 98

EP - 104

JO - Food Chemistry

JF - Food Chemistry

ER -

Identification of a novel ACE-inhibitory peptide from casein and evaluation of the inhibitory mechanisms

Abstract

Keywords

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