Nordihydroguaiaretic acid prevents glycation induced structural alterations and aggregation of albumin

This study demonstrates the antiglycation activity of Nordihydroguaiaretic acid, a lignin from the creosote bush (Larrea tridentate), which has also been proven to assist in the treatment of cancer, neurological disorders, and cardiovascular complications. We determined the antiglycation activity of...

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Bibliographic Details
Published in:International journal of biological macromolecules 2019-02, Vol.122, p.479-484
Main Authors: Awasthi, Saurabh, Preethy, R., Saraswathi, N.T.
Format: Article
Language:English
Subjects:
Aggregation
Animals
Cattle
Glycosylation - drug effects
Maillard reaction
Masoprocol - metabolism
Masoprocol - pharmacology
Molecular Docking Simulation
Nordihydroguaiaretic acid
Protein Aggregates - drug effects
Protein Conformation
Serum Albumin, Bovine - chemistry
Serum Albumin, Bovine - metabolism
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Summary:This study demonstrates the antiglycation activity of Nordihydroguaiaretic acid, a lignin from the creosote bush (Larrea tridentate), which has also been proven to assist in the treatment of cancer, neurological disorders, and cardiovascular complications. We determined the antiglycation activity of NDG based on spectroscopic analysis, molecular interactions and circular dichroism studies with albumin. It was also seen that NDG inhibits the aggregation of albumin, after glycation, using Thioflavin T binding and confocal imaging. Results suggest that NDG is a potent inhibitor of advanced glycation end products formation. NDG was found to impart protective effects on albumin by preventing glycation modification of lysine residues (Lys20, Phe36, Lys41, Lys131, and Lys132) due to glycation. [Display omitted] •NDG prevented the formation of both early and advanced glycation end products.•NDG inhibited glycation induced aggregation of albumin.•Circular dichroism analysis suggested the protective effects of NDG towards the native albumin structure.•Molecular interaction studies revealed that NDG binds to albumin with high affinity.
ISSN:0141-8130
1879-0003
DOI:10.1016/j.ijbiomac.2018.10.173