Prunin from Poncirus trifoliata (L.) Rafin Inhibits Aldose Reductase and Glucose-Fructose-Mediated Protein Glycation and Oxidation of Human Serum Albumin

Md Yousof Ali; Gerald W. Zamponi; Qudeer Ahmed Abdul; Su Hui Seong; Byung Sun Min; Hyun Ah Jung; Jae Sue Choi

doi:10.1021/acs.jafc.3c09716

Prunin from Poncirus trifoliata (L.) Rafin Inhibits Aldose Reductase and Glucose-Fructose-Mediated Protein Glycation and Oxidation of Human Serum Albumin

Md Yousof Ali
, Gerald W. Zamponi
, Qudeer Ahmed Abdul
, Su Hui Seong
, Byung Sun Min
, Hyun Ah Jung^*
, Jae Sue Choi^*

^*Corresponding author for this work

Department of Food Science and Human Nutrition

Research output: Contribution to journal › Journal article › peer-review

2 Scopus citations

Abstract

Diabetes complications are associated with aldose reductase (AR) and advanced glycation end products (AGEs). Using bioassay-guided isolation by column chromatography, 10 flavonoids and one coumarin were isolated from Poncirus trifoliata Rafin and tested in vitro for an inhibitory effect against human recombinant AR (HRAR) and rat lens AR (RLAR). Prunin, narirutin, and naringin inhibited RLAR (IC₅₀ 0.48-2.84 μM) and HRAR (IC₅₀ 0.68-4.88 μM). Docking simulations predicted negative binding energies and interactions with the RLAR and HRAR binding pocket residues. Prunin (0.1 and 12.5 μM) prevented the formation of fluorescent AGEs and nonfluorescent N^ϵ-(carboxymethyl) lysine (CML), as well as the fructose-glucose-mediated protein glycation and oxidation of human serum albumin (HSA). Prunin suppressed the formation of the β-cross-amyloid structure of HSA. These results indicate that prunin inhibits oxidation-dependent protein damage, AGE formation, and AR, which may help prevent diabetes complications.

Original language	English
Pages (from-to)	7203-7218
Number of pages	16
Journal	Journal of Agricultural and Food Chemistry
Volume	72
Issue number	13
DOIs	https://doi.org/10.1021/acs.jafc.3c09716
State	Published - 2024.04.3

UN SDGs

This output contributes to the following UN Sustainable Development Goals (SDGs)

SDG 3 Good Health and Well-being

Keywords

AGEs
aldose reductase
diabetic complications
flavonoids
Poncirus trifoliata (L.) Rafin
protein glycation
prunin

Quacquarelli Symonds(QS) Subject Topics

Agriculture & Forestry
Chemistry

Access to Document

10.1021/acs.jafc.3c09716

Cite this

@article{eaf5f7b1f95e491a9d5aa691b87035aa,

title = "Prunin from Poncirus trifoliata (L.) Rafin Inhibits Aldose Reductase and Glucose-Fructose-Mediated Protein Glycation and Oxidation of Human Serum Albumin",

abstract = "Diabetes complications are associated with aldose reductase (AR) and advanced glycation end products (AGEs). Using bioassay-guided isolation by column chromatography, 10 flavonoids and one coumarin were isolated from Poncirus trifoliata Rafin and tested in vitro for an inhibitory effect against human recombinant AR (HRAR) and rat lens AR (RLAR). Prunin, narirutin, and naringin inhibited RLAR (IC50 0.48-2.84 μM) and HRAR (IC50 0.68-4.88 μM). Docking simulations predicted negative binding energies and interactions with the RLAR and HRAR binding pocket residues. Prunin (0.1 and 12.5 μM) prevented the formation of fluorescent AGEs and nonfluorescent Nϵ-(carboxymethyl) lysine (CML), as well as the fructose-glucose-mediated protein glycation and oxidation of human serum albumin (HSA). Prunin suppressed the formation of the β-cross-amyloid structure of HSA. These results indicate that prunin inhibits oxidation-dependent protein damage, AGE formation, and AR, which may help prevent diabetes complications.",

keywords = "AGEs, aldose reductase, diabetic complications, flavonoids, Poncirus trifoliata (L.) Rafin, protein glycation, prunin",

author = "Ali, \{Md Yousof\} and Zamponi, \{Gerald W.\} and Abdul, \{Qudeer Ahmed\} and Seong, \{Su Hui\} and Min, \{Byung Sun\} and Jung, \{Hyun Ah\} and Choi, \{Jae Sue\}",

note = "Publisher Copyright: {\textcopyright} 2024 American Chemical Society.",

year = "2024",

month = apr,

day = "3",

doi = "10.1021/acs.jafc.3c09716",

language = "English",

volume = "72",

pages = "7203--7218",

journal = "Journal of Agricultural and Food Chemistry",

issn = "0021-8561",

number = "13",

}

Prunin from Poncirus trifoliata (L.) Rafin Inhibits Aldose Reductase and Glucose-Fructose-Mediated Protein Glycation and Oxidation of Human Serum Albumin. / Ali, Md Yousof; Zamponi, Gerald W.; Abdul, Qudeer Ahmed et al.
In: Journal of Agricultural and Food Chemistry, Vol. 72, No. 13, 03.04.2024, p. 7203-7218.

Research output: Contribution to journal › Journal article › peer-review

TY - JOUR

T1 - Prunin from Poncirus trifoliata (L.) Rafin Inhibits Aldose Reductase and Glucose-Fructose-Mediated Protein Glycation and Oxidation of Human Serum Albumin

AU - Ali, Md Yousof

AU - Zamponi, Gerald W.

AU - Abdul, Qudeer Ahmed

AU - Seong, Su Hui

AU - Min, Byung Sun

AU - Jung, Hyun Ah

AU - Choi, Jae Sue

PY - 2024/4/3

Y1 - 2024/4/3

N2 - Diabetes complications are associated with aldose reductase (AR) and advanced glycation end products (AGEs). Using bioassay-guided isolation by column chromatography, 10 flavonoids and one coumarin were isolated from Poncirus trifoliata Rafin and tested in vitro for an inhibitory effect against human recombinant AR (HRAR) and rat lens AR (RLAR). Prunin, narirutin, and naringin inhibited RLAR (IC50 0.48-2.84 μM) and HRAR (IC50 0.68-4.88 μM). Docking simulations predicted negative binding energies and interactions with the RLAR and HRAR binding pocket residues. Prunin (0.1 and 12.5 μM) prevented the formation of fluorescent AGEs and nonfluorescent Nϵ-(carboxymethyl) lysine (CML), as well as the fructose-glucose-mediated protein glycation and oxidation of human serum albumin (HSA). Prunin suppressed the formation of the β-cross-amyloid structure of HSA. These results indicate that prunin inhibits oxidation-dependent protein damage, AGE formation, and AR, which may help prevent diabetes complications.

AB - Diabetes complications are associated with aldose reductase (AR) and advanced glycation end products (AGEs). Using bioassay-guided isolation by column chromatography, 10 flavonoids and one coumarin were isolated from Poncirus trifoliata Rafin and tested in vitro for an inhibitory effect against human recombinant AR (HRAR) and rat lens AR (RLAR). Prunin, narirutin, and naringin inhibited RLAR (IC50 0.48-2.84 μM) and HRAR (IC50 0.68-4.88 μM). Docking simulations predicted negative binding energies and interactions with the RLAR and HRAR binding pocket residues. Prunin (0.1 and 12.5 μM) prevented the formation of fluorescent AGEs and nonfluorescent Nϵ-(carboxymethyl) lysine (CML), as well as the fructose-glucose-mediated protein glycation and oxidation of human serum albumin (HSA). Prunin suppressed the formation of the β-cross-amyloid structure of HSA. These results indicate that prunin inhibits oxidation-dependent protein damage, AGE formation, and AR, which may help prevent diabetes complications.

KW - AGEs

KW - aldose reductase

KW - diabetic complications

KW - flavonoids

KW - Poncirus trifoliata (L.) Rafin

KW - protein glycation

KW - prunin

UR - https://www.scopus.com/pages/publications/85188452469

U2 - 10.1021/acs.jafc.3c09716

DO - 10.1021/acs.jafc.3c09716

M3 - Journal article

C2 - 38518258

AN - SCOPUS:85188452469

SN - 0021-8561

VL - 72

SP - 7203

EP - 7218

JO - Journal of Agricultural and Food Chemistry

JF - Journal of Agricultural and Food Chemistry

IS - 13

ER -

Prunin from Poncirus trifoliata (L.) Rafin Inhibits Aldose Reductase and Glucose-Fructose-Mediated Protein Glycation and Oxidation of Human Serum Albumin

Abstract

UN SDGs

Keywords

Quacquarelli Symonds(QS) Subject Topics

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