Analyzation of the binding mechanism and the isoelectric point of glycated albumin with self-assembled, aptamer-conjugated films by using surface plasmon resonance

Glycated albumin(GA), a biomarker which has great potential to replace glycated hemoglobin in the diagnosis and treatment of diabetes, is being extensively studied by scientists, especially in preventive medicine. Aptamers, as novel probes, have attracted much attention due to their high specificity, wide storage conditions, and simple preparation. However, the interaction mechanism between GA and its aptamer is still unclear, hindering the progress of diabetic aptamer sensors into clinical testing. In this study, the interaction mechanism between GA and its aptamer was evaluated for the first time using surface plasmon resonance by changing the pH value, salt concentration and temperature. The successful preparation of the sensor chip is proved by the water contact angle, Atomic Force Microscope, and the X-ray photoelectron spectroscopy. This study shows that the pH can greatly affect the formation of a complex from the interaction between the aptamer and GA. The interaction mechanism between GA aptamer and GA was caused by electrostatic force. Otherwise, this is the first time to detect protein isoelectric point (pI) using SPR. This study provides an important reference for researchers of aptamer sensors from the perspective of detection environment, and promotes the use of aptamer sensors to the clinic.

Automated summary

This study evaluated for the first time the interaction mechanism between glycated albumin (GA) and its aptamer by changing the pH value, salt concentration, and temperature. The results showed that the pH greatly affected the formation of the complex between the aptamer and GA, and the interaction mechanism was caused by electrostatic force. Additionally, this study also detected the protein isoelectric point (pI) using surface plasmon resonance (SPR) for the first time.