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Inhibition of advanced glycation end products by isoferulic acid and its free radical scavenging capacity: An in vitro and molecular docking study.
Arfin, Sadaf; Siddiqui, Gufran Ahmed; Naeem, Aabgeena; Moin, Shagufta.
Affiliation
  • Arfin S; Department of Biochemistry, JNMC, AMU, Aligarh, India.
  • Siddiqui GA; Department of Biochemistry, F/O Life Sciences, AMU, Aligarh, India.
  • Naeem A; Department of Biochemistry, F/O Life Sciences, AMU, Aligarh, India. Electronic address: anaeem.bc@amu.ac.in.
  • Moin S; Department of Biochemistry, JNMC, AMU, Aligarh, India. Electronic address: shagufta.moin@yahoo.com.
Int J Biol Macromol ; 118(Pt B): 1479-1487, 2018 Oct 15.
Article in En | MEDLINE | ID: mdl-29969636
ABSTRACT
Non-enzymatic glycation and Oxidation of some essential biological macromolecules are paramount in the pathogenesis of various diseases including diabetes and atherosclerosis. Hyperglycemia plays a key role in the pathological process of diabetic complications by progressive accumulation of advanced glycation end products (AGEs) in body tissues. Formation of AGEs as a result of protein glycation is followed by an increased free radical activity that additionally contributes towards the bio-macromolecular damage. The present study aimed to evaluate the free radical scavenging and antiglycation capacity of isoferulic acid (IFA). The free radical scavenging activity of IFA was measured using DPPH, FRAP, and metal chelating assays. IFA showed effective reducing power, free radical scavenging activity and metal chelation activity in concentration dependent manner. The antiglycation activity of IFA was studied using various spectroscopic techniques. The obtained results were validated with free amino, sulfhydryl group, carbonyl content and AGEs formation. Secondary structural alterations were monitored using circular dichroism, morphology of aggregates was analyzed using transmission electron microscopy. Molecular docking reveals the possible binding location of IFA with in the sub-domain IIA of human serum albumin (HSA).
Subject(s)

Full text: 1 Collection: 01-internacional Database: MEDLINE Main subject: Free Radical Scavengers / Cinnamates / Glycation End Products, Advanced / Molecular Docking Simulation Limits: Humans Language: En Journal: Int J Biol Macromol Year: 2018 Document type: Article Affiliation country: India Publication country: HOLANDA / HOLLAND / NETHERLANDS / NL / PAISES BAJOS / THE NETHERLANDS

Full text: 1 Collection: 01-internacional Database: MEDLINE Main subject: Free Radical Scavengers / Cinnamates / Glycation End Products, Advanced / Molecular Docking Simulation Limits: Humans Language: En Journal: Int J Biol Macromol Year: 2018 Document type: Article Affiliation country: India Publication country: HOLANDA / HOLLAND / NETHERLANDS / NL / PAISES BAJOS / THE NETHERLANDS