How human serum albumin‐selective DNA aptamer binds to bovine and canine serum albumins

Abstract

Serum albumin (SA) is the most abundant carrier protein in blood. SA carries a diverse range of nutrients, drugs, and metal ions. It has wide clinical and biochemical applications. Human serum albumin (HSA) can be used as a biomarker for kidney and liver diseases. Aptasensor is one of potential HSA detection methods. HSA-specific aptamer was selected for HSA detection. In animals, bovine serum albumin (BSA) and canine serum albumins (CSA) share high sequence similarities to HSA. Thus, it is interesting to explore the possibility of using HSA-selective aptamer for BSA and CSA aptasensor. In this study, molecular dynamics (MD) simulations were initially employed to investigate the binding of aptamer to BSA and CSA in comparison to HSA. Like HSA, both BSA and CSA can bind aptamer, but different binding affinities are observed. BSA shows the tighter binding to aptamer than CSA. Domain III is found to be the aptamer-binding domain although no specific aptamer conformation is captured. However, in all cases, the aptamer utilizes the 3 0-end to attach on an albumin surface. Both nucleobases and phosphate backbones on a DNA aptamer are important for albumin-aptamer complexation. Our results imply the possibility of using HSA-specific aptamer for BSA detection due to tighter binding observed, but may be less effective in CSA. However, the test in actual complicated condition must be further studied.

Understanding the Influence of Serum Proteins Adsorption on the Mechano‐Bactericidal Efficacy and Immunomodulation of Nanostructured Titanium

“…The structural similarity between BSA and human serum albumin frequently renders it as the preferred model for comparative studies. [33] Following BSA adsorption onto the different Ti surfaces (Figure 2B), the BCA assay indicated a similar adsorption pattern for BSA as previously determined for HSP. As well as more prominent in the HTTi surfaces than that in the pTi surfaces, quantification of adsorbed BSA determined to be a concentration-dependent process.…”

Site-specific DNA functionalization through the tetrazene-forming reaction in ionic liquids

“…A DNA aptamer for human serum albumin was chosen as a model substrate for this study of phosphines. 36 We focused only on reasonably air-stable phosphines including triaryl-phosphines with a range of substituents (2a-2g), alkylphosphine (John-Phos, 2h), and arylphosphite (2i) and used triphenylphosphine oxide (3) as a negative control (Fig. 4A and C).…”

Site-Specific DNA Functionalization through the Tetrazene-Forming Reaction in Ionic Liquids

“…A DNA aptamer for human serum albumin was chosen as a model substrate for this study of phoshines. 32 We focused only on reasonably air-stable phosphines including triaryl-phosphines with a range of substituents (2a-2g), alkylphosphine (JohnPhos, 2h), and aryl phosphite (2i) and used triphenylphosphine oxide (3) as a negative control (Figs. 4A,4C).…”