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Sulfated galactofucan from seaweed Padina tetrastromatica attenuates proteolytic enzyme dipeptidylpeptidase-4: a potential anti-hyperglycemic lead

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Relation http://eprints.cmfri.org.in/15690/
https://www.tandfonline.com/doi/full/10.1080/14786419.2022.2025802
10.1080/14786419.2022.2025802
 
Title Sulfated galactofucan from seaweed Padina tetrastromatica attenuates proteolytic enzyme dipeptidylpeptidase-4: a potential anti-hyperglycemic lead
 
Creator Antony, Tima
Chakraborty, Kajal
Dhara, Subhajit
 
Subject Biochemistry
Seaweed
 
Description Dipeptidyl-peptidase-4 is a multifunctional ectoenzyme, which is implicated with hyperglycemic pathophysiology. Therefore, dipeptidyl-peptidase-4 inhibitors could be used as an attractive therapeutic strategy in blood-glucose homeostasis to attenuate the pathophysiologies of diabetes. A sulfated galactofucan characterized as [!1)-O-4-sulfonato-a-fucopyranosyl-(2!1)-O-2-sulfonatoa-fucopyranose-(3!] along with a branch of [!1)-6-O-methylb-galactopyranosyl-(4!] unit at the C-4 position of O-2-sulfonatoa-fucopyranose, isolated from the seaweed Padina tetrastromatica, exhibited prospective attenuation property against dipeptidylpeptidase-4 (IC50 0.25 mg mL1). The studied sulfated galactofucan exhibited potential inhibitory properties against carbolytic enzymes a-amylase (IC50 0.98 mg mL1) and a-glucosidase (IC500.87 mg mL1) in comparison with the standard antidiabetic agent acarbose, along with radical scavenging activities. The seaweed-originated galactofucan could be developed as a promising natural therapeutic lead against hyperglycemic disorder.
 
Publisher Taylor and Francis
 
Date 2022-01-17
 
Type Article
PeerReviewed
 
Format text
 
Language en
 
Identifier http://eprints.cmfri.org.in/15690/1/Natural%20Product%20Research_2022_Kajal%20Chakraborty.pdf
Antony, Tima and Chakraborty, Kajal and Dhara, Subhajit (2022) Sulfated galactofucan from seaweed Padina tetrastromatica attenuates proteolytic enzyme dipeptidylpeptidase-4: a potential anti-hyperglycemic lead. Natural Product Research. pp. 1-12.