Inhibitory effect of gold nanoparticles on the D-ribose glycation of bovine serum albumin

Weixi Liu,1 Menashi A Cohenford,1–3 Leslie Frost,3 Champika Seneviratne,4 Joel A Dain1 1Department of Chemistry, University of Rhode Island, Kingston, RI, USA; 2Department of Integrated Science and Technology, 3Department of Chemistry, Marshall University, Huntington, WV, USA; 4Department...

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Autores principales: Liu W, Cohenford MA, Frost L, Seneviratne C, Dain JA
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Publicado: Dove Medical Press 2014
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spelling oai:doaj.org-article:838203bcf3ed407bbbca268a0ca0e8392021-12-02T01:34:50ZInhibitory effect of gold nanoparticles on the D-ribose glycation of bovine serum albumin1178-2013https://doaj.org/article/838203bcf3ed407bbbca268a0ca0e8392014-11-01T00:00:00Zhttp://www.dovepress.com/inhibitory-effect-of-gold-nanoparticles-on-the-d-ribose-glycation-of-b-peer-reviewed-article-IJNhttps://doaj.org/toc/1178-2013 Weixi Liu,1 Menashi A Cohenford,1–3 Leslie Frost,3 Champika Seneviratne,4 Joel A Dain1 1Department of Chemistry, University of Rhode Island, Kingston, RI, USA; 2Department of Integrated Science and Technology, 3Department of Chemistry, Marshall University, Huntington, WV, USA; 4Department of Chemistry, College of the North Atlantic, Labrador, NL, Canada Abstract: Formation of advanced glycation end products (AGEs) by nonenzymatic glycation of proteins is a major contributory factor to the pathophysiology of diabetic conditions including senile dementia and atherosclerosis. This study describes the inhibitory effect of gold nanoparticles (GNPs) on the D-ribose glycation of bovine serum albumin (BSA). A combination of analytical methods including ultraviolet–visible spectrometry, high performance liquid chromatography, circular dichroism, and matrix-assisted laser desorption/ionization time-of-flight (MALDI-TOF) mass spectrometry were used to determine the extent of BSA glycation in the presence of citrate reduced spherical GNPs of various sizes and concentrations. GNPs of particle diameters ranging from 2 nm to 20 nm inhibited BSA’s AGE formation. The extent of inhibition correlated with the total surface area of the nanoparticles. GNPs of highest total surface area yielded the most inhibition whereas those with the lowest total surface area inhibited the formation of AGEs the least. Additionally, when GNPs’ total surface areas were set the same, their antiglycation activities were similar. This inhibitory effect of GNPs on BSA’s glycation by D-ribose suggests that colloidal particles may have a therapeutic application for the treatment of diabetes and conditions that promote hyperglycemia. Keywords: gold nanoparticles, glycation, AGEs, GNPs, BSALiu WCohenford MAFrost LSeneviratne CDain JADove Medical PressarticleMedicine (General)R5-920ENInternational Journal of Nanomedicine, Vol 2014, Iss Issue 1, Pp 5461-5469 (2014)
institution DOAJ
collection DOAJ
language EN
topic Medicine (General)
R5-920
spellingShingle Medicine (General)
R5-920
Liu W
Cohenford MA
Frost L
Seneviratne C
Dain JA
Inhibitory effect of gold nanoparticles on the D-ribose glycation of bovine serum albumin
description Weixi Liu,1 Menashi A Cohenford,1–3 Leslie Frost,3 Champika Seneviratne,4 Joel A Dain1 1Department of Chemistry, University of Rhode Island, Kingston, RI, USA; 2Department of Integrated Science and Technology, 3Department of Chemistry, Marshall University, Huntington, WV, USA; 4Department of Chemistry, College of the North Atlantic, Labrador, NL, Canada Abstract: Formation of advanced glycation end products (AGEs) by nonenzymatic glycation of proteins is a major contributory factor to the pathophysiology of diabetic conditions including senile dementia and atherosclerosis. This study describes the inhibitory effect of gold nanoparticles (GNPs) on the D-ribose glycation of bovine serum albumin (BSA). A combination of analytical methods including ultraviolet–visible spectrometry, high performance liquid chromatography, circular dichroism, and matrix-assisted laser desorption/ionization time-of-flight (MALDI-TOF) mass spectrometry were used to determine the extent of BSA glycation in the presence of citrate reduced spherical GNPs of various sizes and concentrations. GNPs of particle diameters ranging from 2 nm to 20 nm inhibited BSA’s AGE formation. The extent of inhibition correlated with the total surface area of the nanoparticles. GNPs of highest total surface area yielded the most inhibition whereas those with the lowest total surface area inhibited the formation of AGEs the least. Additionally, when GNPs’ total surface areas were set the same, their antiglycation activities were similar. This inhibitory effect of GNPs on BSA’s glycation by D-ribose suggests that colloidal particles may have a therapeutic application for the treatment of diabetes and conditions that promote hyperglycemia. Keywords: gold nanoparticles, glycation, AGEs, GNPs, BSA
format article
author Liu W
Cohenford MA
Frost L
Seneviratne C
Dain JA
author_facet Liu W
Cohenford MA
Frost L
Seneviratne C
Dain JA
author_sort Liu W
title Inhibitory effect of gold nanoparticles on the D-ribose glycation of bovine serum albumin
title_short Inhibitory effect of gold nanoparticles on the D-ribose glycation of bovine serum albumin
title_full Inhibitory effect of gold nanoparticles on the D-ribose glycation of bovine serum albumin
title_fullStr Inhibitory effect of gold nanoparticles on the D-ribose glycation of bovine serum albumin
title_full_unstemmed Inhibitory effect of gold nanoparticles on the D-ribose glycation of bovine serum albumin
title_sort inhibitory effect of gold nanoparticles on the d-ribose glycation of bovine serum albumin
publisher Dove Medical Press
publishDate 2014
url https://doaj.org/article/838203bcf3ed407bbbca268a0ca0e839
work_keys_str_mv AT liuw inhibitoryeffectofgoldnanoparticlesonthedriboseglycationofbovineserumalbumin
AT cohenfordma inhibitoryeffectofgoldnanoparticlesonthedriboseglycationofbovineserumalbumin
AT frostl inhibitoryeffectofgoldnanoparticlesonthedriboseglycationofbovineserumalbumin
AT seneviratnec inhibitoryeffectofgoldnanoparticlesonthedriboseglycationofbovineserumalbumin
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