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Cinnamic Acid and Its Derivatives Inhibit Fructose-Mediated Protein Glycation
Cinnamic acid and its derivatives have shown a variety of pharmacologic properties. However, little is known about the antiglycation properties of cinnamic acid and its derivatives. The present study sought to characterize the protein glycation inhibitory activity of cinnamic acid and its derivative...
Autores principales: | , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Molecular Diversity Preservation International (MDPI)
2012
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3291992/ https://www.ncbi.nlm.nih.gov/pubmed/22408423 http://dx.doi.org/10.3390/ijms13021778 |
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author | Adisakwattana, Sirichai Sompong, Weerachat Meeprom, Aramsri Ngamukote, Sathaporn Yibchok-anun, Sirintorn |
author_facet | Adisakwattana, Sirichai Sompong, Weerachat Meeprom, Aramsri Ngamukote, Sathaporn Yibchok-anun, Sirintorn |
author_sort | Adisakwattana, Sirichai |
collection | PubMed |
description | Cinnamic acid and its derivatives have shown a variety of pharmacologic properties. However, little is known about the antiglycation properties of cinnamic acid and its derivatives. The present study sought to characterize the protein glycation inhibitory activity of cinnamic acid and its derivatives in a bovine serum albumin (BSA)/fructose system. The results demonstrated that cinnamic acid and its derivatives significantly inhibited the formation of advanced glycation end products (AGEs) by approximately 11.96–63.36% at a concentration of 1 mM. The strongest inhibitory activity against the formation of AGEs was shown by cinnamic acid. Furthermore, cinnamic acid and its derivatives reduced the level of fructosamine, the formation of N(ɛ)-(carboxymethyl) lysine (CML), and the level of amyloid cross β-structure. Cinnamic acid and its derivatives also prevented oxidative protein damages, including effects on protein carbonyl formation and thiol oxidation of BSA. Our findings may lead to the possibility of using cinnamic acid and its derivatives for preventing AGE-mediated diabetic complications. |
format | Online Article Text |
id | pubmed-3291992 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2012 |
publisher | Molecular Diversity Preservation International (MDPI) |
record_format | MEDLINE/PubMed |
spelling | pubmed-32919922012-03-09 Cinnamic Acid and Its Derivatives Inhibit Fructose-Mediated Protein Glycation Adisakwattana, Sirichai Sompong, Weerachat Meeprom, Aramsri Ngamukote, Sathaporn Yibchok-anun, Sirintorn Int J Mol Sci Article Cinnamic acid and its derivatives have shown a variety of pharmacologic properties. However, little is known about the antiglycation properties of cinnamic acid and its derivatives. The present study sought to characterize the protein glycation inhibitory activity of cinnamic acid and its derivatives in a bovine serum albumin (BSA)/fructose system. The results demonstrated that cinnamic acid and its derivatives significantly inhibited the formation of advanced glycation end products (AGEs) by approximately 11.96–63.36% at a concentration of 1 mM. The strongest inhibitory activity against the formation of AGEs was shown by cinnamic acid. Furthermore, cinnamic acid and its derivatives reduced the level of fructosamine, the formation of N(ɛ)-(carboxymethyl) lysine (CML), and the level of amyloid cross β-structure. Cinnamic acid and its derivatives also prevented oxidative protein damages, including effects on protein carbonyl formation and thiol oxidation of BSA. Our findings may lead to the possibility of using cinnamic acid and its derivatives for preventing AGE-mediated diabetic complications. Molecular Diversity Preservation International (MDPI) 2012-02-08 /pmc/articles/PMC3291992/ /pubmed/22408423 http://dx.doi.org/10.3390/ijms13021778 Text en © 2012 by the authors; licensee Molecular Diversity Preservation International, Basel, Switzerland. http://creativecommons.org/licenses/by/3.0 This article is an open-access article distributed under the terms and conditions of the Creative Commons Attribution license (http://creativecommons.org/licenses/by/3.0/). |
spellingShingle | Article Adisakwattana, Sirichai Sompong, Weerachat Meeprom, Aramsri Ngamukote, Sathaporn Yibchok-anun, Sirintorn Cinnamic Acid and Its Derivatives Inhibit Fructose-Mediated Protein Glycation |
title | Cinnamic Acid and Its Derivatives Inhibit Fructose-Mediated Protein Glycation |
title_full | Cinnamic Acid and Its Derivatives Inhibit Fructose-Mediated Protein Glycation |
title_fullStr | Cinnamic Acid and Its Derivatives Inhibit Fructose-Mediated Protein Glycation |
title_full_unstemmed | Cinnamic Acid and Its Derivatives Inhibit Fructose-Mediated Protein Glycation |
title_short | Cinnamic Acid and Its Derivatives Inhibit Fructose-Mediated Protein Glycation |
title_sort | cinnamic acid and its derivatives inhibit fructose-mediated protein glycation |
topic | Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3291992/ https://www.ncbi.nlm.nih.gov/pubmed/22408423 http://dx.doi.org/10.3390/ijms13021778 |
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