Description
Purpurogallin is a phenol that has been found in
D. divisa and a derivative of pyrogallol that has diverse biological activities, including antimicrobial, antioxidant, and enzyme inhibitory properties. It is active against the Gram-positive bacteria
S. aureus, methicillin-resistant
S. aureus (MRSA),
S. epidermidis, and
B. subtilis (MICs = 11-110 μg/ml), the Gram-negative bacteria
S. marcescens,
P. vulgaris,
K. pneumoniae,
E. coli,
S. typhi, and
E. cloacae (MIC = 110 μg/ml for all), as well as
P. falciparum strain FCB1 clone NC-1 (IC
50 = 55 μM). Purpurogallin (2, 5, and 10 μM) scavenges 2,2-diphenyl-1-picrylhydrazyl (DPPH; ) radicals in a cell-free assay and reduces hydrogen peroxide- and radiation-induced production of reactive oxygen species (ROS) in HaCaT keratinocytes. It inhibits the activity of EGFR, glutathione-S-transferase (GST), prolyl endopeptidase, and glyoxalase I (IC
50s = 27.5, 8, 16, and 50 μM, respectively), as well as catechol O-methyltransferase (COMT; K
i = 0.074 μM), in cell-free assays.
Chemical Properties
BROWN FINE CRYSTALLINE POWDER
Uses
xanthine oxidase inhibitor, antioxidant
Definition
ChEBI: A cyclic ketone that is 5H-benzocycloheptene bearing an oxo group at position 5 and hydroxy groups at positions 2, 3, 4 and 6.
Enzyme inhibitor
This aglycone (FW = 220.18 g/mol) of a number of glycosides (e.g., dryophantin) from several nutgalls. Purpurogallin is a scavenger of polymorphonuclear leukocyte-derived oxyradicals and acts as a cardioprotector. Target(s): catechol O-methyltransferase; cystathionine b-synthase; glutathione-disulfide reductase; glutathione S-transferase; HIV-1 integrase; lactoylglutathione lyase, or glyoxalase I; 3-phosphoglycerate kinase; prolyl endopeptidase; protein-tyrosine kinase; and xanthine oxidase.
References
[1] Y INAMORI. Biological activity of purpurogallin.[J]. Bioscience, Biotechnology, and Biochemistry, 1997, 61 5: 890-892. DOI:
10.1271/bbb.61.890[2] AO XUAN ZHEN. Purpurogallin Protects Keratinocytes from Damage and Apoptosis Induced by Ultraviolet B Radiation and Particulate Matter 2.5.[J]. Biomolecules & Therapeutics, 2019, 27 4: 395-403. DOI:
10.4062/biomolther.2018.151[3] JOHN F. BARNARD John F H David L Vander Jagt. Small molecule probes of glyoxalase I and glyoxalase II[J]. Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology, 1994, 1208 1: Pages 127-135. DOI:
10.1016/0167-4838(94)90169-4[4] M ABOU-KARAM W T S. Inhibition of oncogene product enzyme activity as an approach to cancer chemoprevention. Tyrosine-specific protein kinase inhibition by purpurogallin from Quercus sp. nutgall.[J]. Phytotherapy Research, 1999, 13 4: 337-340. DOI:
10.1002/(sici)1099-1573(199906)13:4<337::aid-ptr451>3.0.co;2-j[5] MUKUL DAS Hasan M David R Bickers. Plant phenols as invitro inhibitors of glutathione S-transferase(s)[J]. Biochemical and biophysical research communications, 1984, 120 2: Pages 427-433. DOI:
10.1016/0006-291x(84)91271-3[6] VESER J. Kinetics and inhibition studies of catechol O-methyltransferase from the yeast Candida tropicalis.[J]. Journal of Bacteriology, 1987, 169 8: 3696-3700. DOI:
10.1128/jb.169.8.3696-3700.1987
