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(A) Cartoon representations of apo HSA (left) and GHSA (right) where two glucose molecules are located at Sudlow site I. The albumin-selective DNA aptamer in a complex with a GQD is shown in (B). Two initial conformations of albumin (front and back) on an aptamer-GQD complex in this work are shown in (C).
Source publication
Diabetes mellitus is a chronic metabolic disease involving continued elevated blood glucose levels. It is a leading cause of mortality and reduced life expectancy. Glycated human serum albumin (GHSA) has been reported to be a potential diabetes biomarker. A nanomaterial-based aptasensor is one of the effective techniques to detect GHSA. Graphene qu...
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... has a heart-like shape composed of 585 amino acids with three homologous domains (I, II, and III). Each domain contains two subdomains (A and B) ( Figure 1A). HSA has two drug sites [Sudlow sites I (warfarin−azapropazone binding site) and II (indole−benzodiazepine binding site)] located inside domains IIA and IIIA ( Figure 1A). ...
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... domain contains two subdomains (A and B) ( Figure 1A). HSA has two drug sites [Sudlow sites I (warfarin−azapropazone binding site) and II (indole−benzodiazepine binding site)] located inside domains IIA and IIIA ( Figure 1A). In the presence of blood glucose, a free amino group on HSA interacts with an aldehyde group on glucose to form an Amadori product. ...
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... Recently, a crystal structure of GHSA has been solved. 57 Two glucose molecules [open-(GLO) and closed-(GLC) forms] were found inside drug site I or Sudlow site I ( Figure 1A). A previous work shows that the GHSA structure gets damaged more than HSA during binding to a bare GQD. ...
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... assemblies of HSA and GHSA to the GQD-aptamer complex (GQDA) are studied in comparison. Two different albumin orientations (front and back poses facing GQDA) are investigated to mimic possible binding poses of albumin onto the aptamer-GQD complex ( Figure 1C). Both front and back orientations used here are based on previously reported ligand-binding sites on an albumin surface. ...
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... This aptamer shows high selectivity for GHSA than other abundant proteins such as IgG and Hb in blood. 52 This single-stranded DNA aptamer contains 23 nucleotides comprising 5'-TGCGGTTGTAGTACTCGTGGCCG-3′ ( Figure 1C). A GQD sheet has a dimension of 48 Å × 42 Å constructed by a Nanotube Builder module implemented in the Visual Molecular Dynamics (VMD) program. ...
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... The GQD-aptamer complex (GQDA) was taken from a previous study, 67 where the GQD-aptamer complex used here was obtained from the 200 ns final snapshot of a GQD-aptamer assembly. For each albumin, two systems where a GQD-aptamer was placed at a distance of 10 Å from the back (B) and front (F) of a protein were set (see Figure 1C for initial configurations). The infixes of "-F" and "-B" refer to the GQDA position. ...
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... In addition, the structural drift and fluctuation of HSA and GHSA are measured via the rootmean-square deviations (RMSDs) and root-mean-square fluctuations (RMSFs) of all C-alpha atoms (Figure 2C,D). RMSDs of all systems are shown in Figure S1 in the Supplementary Information. Overall, HSA shows slightly higher structural flexibility than GHSA in both front and back binding poses ( Figure 2C). ...
