Monohydroxamates of Aspartic Acid and Glutamic Acid Exhibit Antioxidant and Angiotensin Converting Enzyme Inhibitory Activities

Der Zen Liu, Yin Shiou Lin, Wen Chi Hou

研究成果: 雜誌貢獻文章

26 引文 (Scopus)

摘要

Two monohydroxamates of L-aspartic acid β-hydroxamate (AAH) and L-glutamic acid γ-hydroxamate (GAH) were used for testing antioxidant and angiotensin converting enzyme (ACE) inhibitory activities in comparison with those of asparagine and glutamine, respectively. The half-inhibition concentrations, IC50, of scavenging activity against 1,1-diphenyl-2-picrylhydrazyl (DPPH) were 36 and 48 μM and against superoxide radicals were 18.99 and 6.33 mM, respectively, for AAH and GAH. However, no activities of asparagine and glutamine were found. AAH and GAH also exhibited activities against peroxynitrite-mediated dihydrorhodamine 123 oxidations and hydroxyl radical-mediated DNA damage. For ACE inhibitory activities, the IC50 values were 4.92 and 6.56 mM, respectively, for AAH and GAH. The ACE hydrolyzed products on the TLC chromatogram also confirmed the inhibitory activities of the two amino acid hydroxamates on ACE. When 1.23 mM AAH was added, AAH showed competitive inhibitions against ACE, and the apparent inhibition constant (Ki) was 2.20 mM.

原文英語
頁(從 - 到)2386-2390
頁數5
期刊Journal of Agricultural and Food Chemistry
52
發行號8
DOIs
出版狀態已發佈 - 四月 21 2004

指紋

peptidyl-dipeptidase A
Enzyme activity
Peptidyl-Dipeptidase A
aspartic acid
glutamic acid
Aspartic Acid
Glutamic Acid
Antioxidants
antioxidants
Asparagine
asparagine
Glutamine
glutamine
Inhibitory Concentration 50
inhibitory concentration 50
Peroxynitrous Acid
Scavenging
hydroxyl radicals
Superoxides
Hydroxyl Radical

ASJC Scopus subject areas

  • Agricultural and Biological Sciences (miscellaneous)
  • Food Science
  • Chemistry (miscellaneous)

引用此文

@article{22fe8478f3364a769062436f045ab909,
title = "Monohydroxamates of Aspartic Acid and Glutamic Acid Exhibit Antioxidant and Angiotensin Converting Enzyme Inhibitory Activities",
abstract = "Two monohydroxamates of L-aspartic acid β-hydroxamate (AAH) and L-glutamic acid γ-hydroxamate (GAH) were used for testing antioxidant and angiotensin converting enzyme (ACE) inhibitory activities in comparison with those of asparagine and glutamine, respectively. The half-inhibition concentrations, IC50, of scavenging activity against 1,1-diphenyl-2-picrylhydrazyl (DPPH) were 36 and 48 μM and against superoxide radicals were 18.99 and 6.33 mM, respectively, for AAH and GAH. However, no activities of asparagine and glutamine were found. AAH and GAH also exhibited activities against peroxynitrite-mediated dihydrorhodamine 123 oxidations and hydroxyl radical-mediated DNA damage. For ACE inhibitory activities, the IC50 values were 4.92 and 6.56 mM, respectively, for AAH and GAH. The ACE hydrolyzed products on the TLC chromatogram also confirmed the inhibitory activities of the two amino acid hydroxamates on ACE. When 1.23 mM AAH was added, AAH showed competitive inhibitions against ACE, and the apparent inhibition constant (Ki) was 2.20 mM.",
keywords = "Angiotensin converting enzyme (ACE), Antioxidant activity, L-aspartic acid β-hydroxamate (AAH), L-glutamic acid γ-hydroxamate (GAH)",
author = "Liu, {Der Zen} and Lin, {Yin Shiou} and Hou, {Wen Chi}",
year = "2004",
month = "4",
day = "21",
doi = "10.1021/jf035493g",
language = "English",
volume = "52",
pages = "2386--2390",
journal = "Journal of Agricultural and Food Chemistry",
issn = "0021-8561",
publisher = "American Chemical Society",
number = "8",

}

TY - JOUR

T1 - Monohydroxamates of Aspartic Acid and Glutamic Acid Exhibit Antioxidant and Angiotensin Converting Enzyme Inhibitory Activities

AU - Liu, Der Zen

AU - Lin, Yin Shiou

AU - Hou, Wen Chi

PY - 2004/4/21

Y1 - 2004/4/21

N2 - Two monohydroxamates of L-aspartic acid β-hydroxamate (AAH) and L-glutamic acid γ-hydroxamate (GAH) were used for testing antioxidant and angiotensin converting enzyme (ACE) inhibitory activities in comparison with those of asparagine and glutamine, respectively. The half-inhibition concentrations, IC50, of scavenging activity against 1,1-diphenyl-2-picrylhydrazyl (DPPH) were 36 and 48 μM and against superoxide radicals were 18.99 and 6.33 mM, respectively, for AAH and GAH. However, no activities of asparagine and glutamine were found. AAH and GAH also exhibited activities against peroxynitrite-mediated dihydrorhodamine 123 oxidations and hydroxyl radical-mediated DNA damage. For ACE inhibitory activities, the IC50 values were 4.92 and 6.56 mM, respectively, for AAH and GAH. The ACE hydrolyzed products on the TLC chromatogram also confirmed the inhibitory activities of the two amino acid hydroxamates on ACE. When 1.23 mM AAH was added, AAH showed competitive inhibitions against ACE, and the apparent inhibition constant (Ki) was 2.20 mM.

AB - Two monohydroxamates of L-aspartic acid β-hydroxamate (AAH) and L-glutamic acid γ-hydroxamate (GAH) were used for testing antioxidant and angiotensin converting enzyme (ACE) inhibitory activities in comparison with those of asparagine and glutamine, respectively. The half-inhibition concentrations, IC50, of scavenging activity against 1,1-diphenyl-2-picrylhydrazyl (DPPH) were 36 and 48 μM and against superoxide radicals were 18.99 and 6.33 mM, respectively, for AAH and GAH. However, no activities of asparagine and glutamine were found. AAH and GAH also exhibited activities against peroxynitrite-mediated dihydrorhodamine 123 oxidations and hydroxyl radical-mediated DNA damage. For ACE inhibitory activities, the IC50 values were 4.92 and 6.56 mM, respectively, for AAH and GAH. The ACE hydrolyzed products on the TLC chromatogram also confirmed the inhibitory activities of the two amino acid hydroxamates on ACE. When 1.23 mM AAH was added, AAH showed competitive inhibitions against ACE, and the apparent inhibition constant (Ki) was 2.20 mM.

KW - Angiotensin converting enzyme (ACE)

KW - Antioxidant activity

KW - L-aspartic acid β-hydroxamate (AAH)

KW - L-glutamic acid γ-hydroxamate (GAH)

UR - http://www.scopus.com/inward/record.url?scp=1842783640&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=1842783640&partnerID=8YFLogxK

U2 - 10.1021/jf035493g

DO - 10.1021/jf035493g

M3 - Article

C2 - 15080651

AN - SCOPUS:1842783640

VL - 52

SP - 2386

EP - 2390

JO - Journal of Agricultural and Food Chemistry

JF - Journal of Agricultural and Food Chemistry

SN - 0021-8561

IS - 8

ER -