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Methylglyoxal produces more changes in biochemical and biophysical properties of human IgG under high glucose compared to normal glucose level
Hyperglycaemia triggers increased production of methylglyoxal which can cause gross modification in proteins’ structure vis-a-vis function though advanced glycation end products (AGEs). The AGEs may initiate vascular and nonvascular pathologies. In this study, we have examined the biochemical and bi...
Autores principales: | , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Public Library of Science
2018
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5774746/ https://www.ncbi.nlm.nih.gov/pubmed/29351321 http://dx.doi.org/10.1371/journal.pone.0191014 |
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author | Khan, Mohd Adnan Arif, Zarina Khan, Mohd Asad Moinuddin, Alam, Khursheed |
author_facet | Khan, Mohd Adnan Arif, Zarina Khan, Mohd Asad Moinuddin, Alam, Khursheed |
author_sort | Khan, Mohd Adnan |
collection | PubMed |
description | Hyperglycaemia triggers increased production of methylglyoxal which can cause gross modification in proteins’ structure vis-a-vis function though advanced glycation end products (AGEs). The AGEs may initiate vascular and nonvascular pathologies. In this study, we have examined the biochemical and biophysical changes in human IgG under normal and high glucose after introducing methylglyoxal into the assay mixture. This non-enzymatic reaction mainly engaged lysine residues as indicated by TNBS results. The UV results showed hyperchromicity in modified-IgG samples while fluorescence data supported AGEs formation during the course of reaction. Shift in amide I and amide II band position indicated perturbations in secondary structure. Increase carbonyl content and decrease in sulfhydryl suggests that the modification is accompanied by oxidative stress. All modified-IgG samples showed more thermostability than native IgG; the highest Tm was shown by IgG-high glucose-MGO variant. Results of ANS, Congo red and Thioflavin T dyes clearly suggest increase in hydrophobic patches and aggregation, respectively. SEM and TEM images support aggregates generation in modified-IgG samples. |
format | Online Article Text |
id | pubmed-5774746 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2018 |
publisher | Public Library of Science |
record_format | MEDLINE/PubMed |
spelling | pubmed-57747462018-02-05 Methylglyoxal produces more changes in biochemical and biophysical properties of human IgG under high glucose compared to normal glucose level Khan, Mohd Adnan Arif, Zarina Khan, Mohd Asad Moinuddin, Alam, Khursheed PLoS One Research Article Hyperglycaemia triggers increased production of methylglyoxal which can cause gross modification in proteins’ structure vis-a-vis function though advanced glycation end products (AGEs). The AGEs may initiate vascular and nonvascular pathologies. In this study, we have examined the biochemical and biophysical changes in human IgG under normal and high glucose after introducing methylglyoxal into the assay mixture. This non-enzymatic reaction mainly engaged lysine residues as indicated by TNBS results. The UV results showed hyperchromicity in modified-IgG samples while fluorescence data supported AGEs formation during the course of reaction. Shift in amide I and amide II band position indicated perturbations in secondary structure. Increase carbonyl content and decrease in sulfhydryl suggests that the modification is accompanied by oxidative stress. All modified-IgG samples showed more thermostability than native IgG; the highest Tm was shown by IgG-high glucose-MGO variant. Results of ANS, Congo red and Thioflavin T dyes clearly suggest increase in hydrophobic patches and aggregation, respectively. SEM and TEM images support aggregates generation in modified-IgG samples. Public Library of Science 2018-01-19 /pmc/articles/PMC5774746/ /pubmed/29351321 http://dx.doi.org/10.1371/journal.pone.0191014 Text en © 2018 Khan et al http://creativecommons.org/licenses/by/4.0/ This is an open access article distributed under the terms of the Creative Commons Attribution License (http://creativecommons.org/licenses/by/4.0/) , which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are credited. |
spellingShingle | Research Article Khan, Mohd Adnan Arif, Zarina Khan, Mohd Asad Moinuddin, Alam, Khursheed Methylglyoxal produces more changes in biochemical and biophysical properties of human IgG under high glucose compared to normal glucose level |
title | Methylglyoxal produces more changes in biochemical and biophysical properties of human IgG under high glucose compared to normal glucose level |
title_full | Methylglyoxal produces more changes in biochemical and biophysical properties of human IgG under high glucose compared to normal glucose level |
title_fullStr | Methylglyoxal produces more changes in biochemical and biophysical properties of human IgG under high glucose compared to normal glucose level |
title_full_unstemmed | Methylglyoxal produces more changes in biochemical and biophysical properties of human IgG under high glucose compared to normal glucose level |
title_short | Methylglyoxal produces more changes in biochemical and biophysical properties of human IgG under high glucose compared to normal glucose level |
title_sort | methylglyoxal produces more changes in biochemical and biophysical properties of human igg under high glucose compared to normal glucose level |
topic | Research Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5774746/ https://www.ncbi.nlm.nih.gov/pubmed/29351321 http://dx.doi.org/10.1371/journal.pone.0191014 |
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