Abstract

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.

Highlights

  • Diabetes is one of the most severe pathological conditions worldwide with 422 million afflicted patients, and this figure is rising dramatically, resulting in both health and economic challenges [1]

  • Glycated protein indicates an average amount of free glucose in the blood for an extended period, whereas the free glucose level may vary in the blood throughout the day [3]

  • The Schiff base undergoes tautomeric rearrangement to form ‘Amadori products’. These products are called the crosslinkers of the protein and glycosylating agents, generating advanced glycation end products (AGEs) (Figure 1), which in turn have several health implications [4]

Read more

Summary

Introduction

Diabetes is one of the most severe pathological conditions worldwide with 422 million afflicted patients, and this figure is rising dramatically, resulting in both health and economic challenges [1]. A label-free electrochemical detection method was developed for the determination of various protein concentrations in the solution in the presence or absence of glucose.

Results
Conclusion
Full Text
Published version (Free)

Talk to us

Join us for a 30 min session where you can share your feedback and ask us any queries you have

Schedule a call