Galloylated catechins as potent inhibitors of angiotensin converting enzyme

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3 Citations (Scopus)

Abstract

In the present study, we investigated the inhibitory effects of four tea catechins, including (-)-epicatechin (EC), (-)-epigallocatechin (EGC), (-)-epicatechin gallate (ECg) and (-)-epigallocatechin gallate (EGCg), on angiotensin converting enzyme (ACE) activity in vitro. Each catechin treatment significantly reduced the ACE activity with the order of potency being EGCg > ECg > EGC = EC. The addition of 1 mM borate significantly recovered the reduced ACE activities by tea catechins, suggesting that hydroxyl groups at the B-ring or at a galloyl moiety play an important role in the ACE-inhibitory mechanism. The covalent modification of ACE by tea catechins was also observed by a redox-cycling staining experiment. A Lineweaver-Burk plot indicated that EGC and ECg were noncompetitive inhibitors. The galloylated catechins might more potently inhibit ACE activity in an allosteric manner through the interaction of the galloyl moiety with the non-catalytic site of ACE.

Original languageEnglish
Pages (from-to)847-851
Number of pages5
JournalFood Science and Technology Research
Volume22
Issue number6
DOIs
Publication statusPublished - 2016

Fingerprint

Catechin
peptidyl-dipeptidase A
Enzyme activity
Peptidyl-Dipeptidase A
flavanols
Angiotensin-Converting Enzyme Inhibitors
epigallocatechin
Enzymes
epicatechin
Tea
enzyme activity
tea
borates
Borates
angiotensin-converting enzyme inhibitors
Inhibitor
catechin
Hydroxyl Radical
Oxidation-Reduction
Staining and Labeling

Keywords

  • Angiotensin converting enzyme
  • Covalent modification
  • Non-competitive inhibition
  • Tea catechins

ASJC Scopus subject areas

  • Biotechnology
  • Food Science
  • Chemical Engineering(all)
  • Marketing
  • Industrial and Manufacturing Engineering

Cite this

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title = "Galloylated catechins as potent inhibitors of angiotensin converting enzyme",
abstract = "In the present study, we investigated the inhibitory effects of four tea catechins, including (-)-epicatechin (EC), (-)-epigallocatechin (EGC), (-)-epicatechin gallate (ECg) and (-)-epigallocatechin gallate (EGCg), on angiotensin converting enzyme (ACE) activity in vitro. Each catechin treatment significantly reduced the ACE activity with the order of potency being EGCg > ECg > EGC = EC. The addition of 1 mM borate significantly recovered the reduced ACE activities by tea catechins, suggesting that hydroxyl groups at the B-ring or at a galloyl moiety play an important role in the ACE-inhibitory mechanism. The covalent modification of ACE by tea catechins was also observed by a redox-cycling staining experiment. A Lineweaver-Burk plot indicated that EGC and ECg were noncompetitive inhibitors. The galloylated catechins might more potently inhibit ACE activity in an allosteric manner through the interaction of the galloyl moiety with the non-catalytic site of ACE.",
keywords = "Angiotensin converting enzyme, Covalent modification, Non-competitive inhibition, Tea catechins",
author = "Zhe Liu and Toshiyuki Nakamura and Shintaro Munemasa and Yoshiyuki Murata and Yoshimasa Nakamura",
year = "2016",
doi = "10.3136/fstr.22.847",
language = "English",
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pages = "847--851",
journal = "Food Science and Technology Research",
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TY - JOUR

T1 - Galloylated catechins as potent inhibitors of angiotensin converting enzyme

AU - Liu, Zhe

AU - Nakamura, Toshiyuki

AU - Munemasa, Shintaro

AU - Murata, Yoshiyuki

AU - Nakamura, Yoshimasa

PY - 2016

Y1 - 2016

N2 - In the present study, we investigated the inhibitory effects of four tea catechins, including (-)-epicatechin (EC), (-)-epigallocatechin (EGC), (-)-epicatechin gallate (ECg) and (-)-epigallocatechin gallate (EGCg), on angiotensin converting enzyme (ACE) activity in vitro. Each catechin treatment significantly reduced the ACE activity with the order of potency being EGCg > ECg > EGC = EC. The addition of 1 mM borate significantly recovered the reduced ACE activities by tea catechins, suggesting that hydroxyl groups at the B-ring or at a galloyl moiety play an important role in the ACE-inhibitory mechanism. The covalent modification of ACE by tea catechins was also observed by a redox-cycling staining experiment. A Lineweaver-Burk plot indicated that EGC and ECg were noncompetitive inhibitors. The galloylated catechins might more potently inhibit ACE activity in an allosteric manner through the interaction of the galloyl moiety with the non-catalytic site of ACE.

AB - In the present study, we investigated the inhibitory effects of four tea catechins, including (-)-epicatechin (EC), (-)-epigallocatechin (EGC), (-)-epicatechin gallate (ECg) and (-)-epigallocatechin gallate (EGCg), on angiotensin converting enzyme (ACE) activity in vitro. Each catechin treatment significantly reduced the ACE activity with the order of potency being EGCg > ECg > EGC = EC. The addition of 1 mM borate significantly recovered the reduced ACE activities by tea catechins, suggesting that hydroxyl groups at the B-ring or at a galloyl moiety play an important role in the ACE-inhibitory mechanism. The covalent modification of ACE by tea catechins was also observed by a redox-cycling staining experiment. A Lineweaver-Burk plot indicated that EGC and ECg were noncompetitive inhibitors. The galloylated catechins might more potently inhibit ACE activity in an allosteric manner through the interaction of the galloyl moiety with the non-catalytic site of ACE.

KW - Angiotensin converting enzyme

KW - Covalent modification

KW - Non-competitive inhibition

KW - Tea catechins

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