▎ 摘　　要

Diabetes mellitusis a chronic metabolic disease involving continuedelevated blood glucose levels. It is a leading cause of mortalityand reduced life expectancy. Glycated human serum albumin (GHSA) hasbeen reported to be a potential diabetes biomarker. A nanomaterial-basedaptasensor is one of the effective techniques to detect GHSA. Graphenequantum dots (GQDs) have been widely used in aptasensors as an aptamerfluorescence quencher due to their high biocompatibility and sensitivity.GHSA-selective fluorescent aptamers are first quenched upon bindingto GQDs. The presence of albumin targets results in the release ofaptamers to albumin and consequently fluorescence recovery. To date,the molecular details on how GQDs interact with GHSA-selective aptamersand albumin remain limited, especially the interactions of an aptamer-boundGQD (GQDA) with an albumin. Thus, in this work, molecular dynamicssimulations were used to reveal the binding mechanism of human serumalbumin (HSA) and GHSA to GQDA. The results show the rapid and spontaneousassembly of albumin and GQDA. Multiple sites of albumins can accommodateboth aptamers and GQDs. This suggests that the saturation of aptamerson GQDs is required for accurate albumin detection. Guanine and thymineare keys for albumin-aptamer clustering. GHSA gets denatured morethan HSA. The presence of bound GQDA on GHSA widens the entrance ofdrug site I, resulting in the release of open-chain glucose. The insightobtained here will serve as a base for accurate GQD-based aptasensordesign and development.