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An Electrochemical Chip to Monitor In Vitro Glycation of Proteins and Screening of Antiglycation Potential of Drugs
Hyperglycemia and the production of advanced glycation end products (AGEs) are the primary factors for the development of chronic complications in diabetes. The level of protein glycation is proportional to the glucose concentration and represents mean glycemia. In this study, we present an electroc...
Autores principales: | , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
MDPI
2020
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7690698/ https://www.ncbi.nlm.nih.gov/pubmed/33113943 http://dx.doi.org/10.3390/pharmaceutics12111011 |
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author | Khan, Zeeshan A. Park, Seungkyung |
author_facet | Khan, Zeeshan A. Park, Seungkyung |
author_sort | Khan, Zeeshan A. |
collection | PubMed |
description | Hyperglycemia and the production of advanced glycation end products (AGEs) are the primary factors for the development of chronic complications in diabetes. The level of protein glycation is proportional to the glucose concentration and represents mean glycemia. In this study, we present an electrochemical chip-based method for in vitro glycation monitoring and the efficacy evaluation of an antiglycation compound. An electrochemical chip consisting of five microchambers and embedded microelectrodes was designed for parallel measurements of capacitance signals from multiple solutions at different concentrations. The feasibility of glycation monitoring was then investigated by measuring the capacitance signal at 0.13 MHz with bovine serum albumin and gelatin samples in the presence of various glucose concentrations over 28 days. A significant change in the capacitance due to protein glycation was observed through measurements conducted within 30 s and 21 days of incubation. Finally, we demonstrated that the chip-based capacitance measurement can be utilized for the selection of an antiglycation compound by supplementing the protein solution and hyperglycemic concentration of glucose with an inhibitory concentration of the standard antiglycation agent aspirin. The lack of a significant change in the capacitance over 28 days proved that aspirin is capable of inhibiting protein glycation. Thus, a strong relationship exists between glycation and capacitance, suggesting the application of an electrochemical chip for evaluating glycation and novel antiglycation agents. |
format | Online Article Text |
id | pubmed-7690698 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2020 |
publisher | MDPI |
record_format | MEDLINE/PubMed |
spelling | pubmed-76906982020-11-27 An Electrochemical Chip to Monitor In Vitro Glycation of Proteins and Screening of Antiglycation Potential of Drugs Khan, Zeeshan A. Park, Seungkyung Pharmaceutics Article Hyperglycemia and the production of advanced glycation end products (AGEs) are the primary factors for the development of chronic complications in diabetes. The level of protein glycation is proportional to the glucose concentration and represents mean glycemia. In this study, we present an electrochemical chip-based method for in vitro glycation monitoring and the efficacy evaluation of an antiglycation compound. An electrochemical chip consisting of five microchambers and embedded microelectrodes was designed for parallel measurements of capacitance signals from multiple solutions at different concentrations. The feasibility of glycation monitoring was then investigated by measuring the capacitance signal at 0.13 MHz with bovine serum albumin and gelatin samples in the presence of various glucose concentrations over 28 days. A significant change in the capacitance due to protein glycation was observed through measurements conducted within 30 s and 21 days of incubation. Finally, we demonstrated that the chip-based capacitance measurement can be utilized for the selection of an antiglycation compound by supplementing the protein solution and hyperglycemic concentration of glucose with an inhibitory concentration of the standard antiglycation agent aspirin. The lack of a significant change in the capacitance over 28 days proved that aspirin is capable of inhibiting protein glycation. Thus, a strong relationship exists between glycation and capacitance, suggesting the application of an electrochemical chip for evaluating glycation and novel antiglycation agents. MDPI 2020-10-23 /pmc/articles/PMC7690698/ /pubmed/33113943 http://dx.doi.org/10.3390/pharmaceutics12111011 Text en © 2020 by the authors. Licensee MDPI, Basel, Switzerland. This article is an open access article distributed under the terms and conditions of the Creative Commons Attribution (CC BY) license (http://creativecommons.org/licenses/by/4.0/). |
spellingShingle | Article Khan, Zeeshan A. Park, Seungkyung An Electrochemical Chip to Monitor In Vitro Glycation of Proteins and Screening of Antiglycation Potential of Drugs |
title | An Electrochemical Chip to Monitor In Vitro Glycation of Proteins and Screening of Antiglycation Potential of Drugs |
title_full | An Electrochemical Chip to Monitor In Vitro Glycation of Proteins and Screening of Antiglycation Potential of Drugs |
title_fullStr | An Electrochemical Chip to Monitor In Vitro Glycation of Proteins and Screening of Antiglycation Potential of Drugs |
title_full_unstemmed | An Electrochemical Chip to Monitor In Vitro Glycation of Proteins and Screening of Antiglycation Potential of Drugs |
title_short | An Electrochemical Chip to Monitor In Vitro Glycation of Proteins and Screening of Antiglycation Potential of Drugs |
title_sort | electrochemical chip to monitor in vitro glycation of proteins and screening of antiglycation potential of drugs |
topic | Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7690698/ https://www.ncbi.nlm.nih.gov/pubmed/33113943 http://dx.doi.org/10.3390/pharmaceutics12111011 |
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