Improving aptamer performance: key factors and strategies

Yang, Hong; Zhu, Jiangxiong; Shen, Guoqing; Deng, Yun; Geng, Xueqing; Huang, Weiwen

doi:10.1007/s00604-023-05836-6

Cited by 26 publications

(3 citation statements)

References 122 publications

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“…This conformational change is critical as it brings the aptamer’s nucleotides into proximity with the Aβ oligomer, allowing for hydrogen bonding and electrostatic interactions. Third, the binding is stabilized by various non-covalent interactions, such as hydrogen bonds, van der Waals forces, and electrostatic attractions ( Yu et al, 2023 ). These interactions ensure that the aptamer remains tightly bound to the Aβ oligomer.…”

Section: Discussionmentioning

confidence: 99%

Oligomeric amyloid-β targeted contrast agent for MRI evaluation of Alzheimer’s disease mouse models

Park,

Tian,

Kim

et al. 2024

Front. Pharmacol.

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BackgroundOligomeric amyloid beta (oAβ) is a toxic factor that acts in the early stage of Alzheimer’s disease (AD) and may initiate the pathologic cascade. Therefore, detecting oAβ has a crucial role in the early diagnosis, monitoring, and treatment of AD.PurposeThe purpose of this study was to evaluate MRI signal changes in different mouse models and the time-dependent signal changes using our novel gadolinium (Gd)-dodecane tetraacetic acid (DOTA)- ob5 aptamer contrast agent.MethodsWe developed an MRI contrast agent by conjugating Gd-DOTA-DNA aptamer called ob5 to evaluate its ability to detect oAβ deposits in the brain using MRI. A total of 10 control mice, 9 3xTg AD mice, and 11 APP/PS/Tau AD mice were included in this study, with the age of each model being 16 or 36 weeks. A T1-weighted image was acquired at the time points before (0 min) and after injection of the contrast agent at 5, 10, 15, 20, and 25 min. The analyses were performed to compare MRI signal differences among the three groups and the time-dependent signal differences in different mouse models.ResultsBoth 3xTg AD and APP/PS/Tau AD mouse models had higher signal enhancement than control mice at all scan-time points after injection of our contrast media, especially in bilateral hippocampal areas. In particular, all Tg AD mouse models aged 16 weeks showed a higher contrast enhancement than those aged 36 weeks. For 3xTg AD and APP/PS/Tau AD groups, the signal enhancement was significantly different among the five time points (0 min, 5 min, 10 min, 15 min, 20 min, and 25 min) in multiple ROI areas, typically in the bilateral hippocampus, left thalamus, and left amygdala.ConclusionThe findings of this study suggest that the expression of the contrast agent in different AD models demonstrates its translational flexibility across different species. The signal enhancement peaked around 15–20 min after injection of the contrast agent. Therefore, our novel contrast agent targeting oAβ has the potential ability to diagnose early AD and monitor the progression of AD.

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Section: Discussionmentioning

confidence: 99%

Oligomeric amyloid-β targeted contrast agent for MRI evaluation of Alzheimer’s disease mouse models

Park,

Tian,

Kim

et al. 2024

Front. Pharmacol.

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“…Meanwhile, the UHA-2 aptamer can be rapidly obtained in vitro and has simpler structure and smaller size than conventional antibodies. Due to its high modifiability, the aptamer is greatly expected to show improved inhibition efficiency and stability in vivo , such as with truncation, extension, mutagenesis and modification of aptamer, and use of locked nucleic acids (LNAs). − …”

Section: Discussionmentioning

confidence: 99%

A Universal Aptamer for Influenza A Viruses: Selection, Recognition, and Infection Inhibition

Wang,

Hao,

Huangfu

et al. 2023

ACS Pharmacol. Transl. Sci.

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It is crucial to develop universal inhibitors for viral inhibition due to the rapid mutation of viruses. Herein, a universal aptamer inhibitor was developed that enabled a single DNA molecule to recognize several hemeagglutinin (HA) protein subtypes, inducing broad neutralization against influenza A viruses (IAVs). Through a multi-channel enrichment (MCE) strategy, a highaffinity aptamer named UHA-2 was obtained, with its dissociation constants (K d ) for three different HA proteins being 1.5 ± 0.2 nM (H5N1), 3.7 ± 0.4 nM (H7N9), and 10.1 ± 1.1 nM (H9N2). The UHA-2 aptamer had a universal inhibition effect, by which it could broadly neutralize influenza A H5N1, H7N9, H9N2, H1N1, and H3N2 viruses. Universal aptamer inhibitors have the advantages of acquisition in vitro, stability, simple structure, small size, etc. This study not only develops a novel universal aptamer to achieve a broad inhibition effect on various IAVs, but also opens up an efficient strategy for the development of universal inhibitors against viruses.

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“…Aptamers are short strands of ssDNA or RNA, generally 15-90 nt in length with secondary structures such as hairpins and pseudoknots, and molecular weights of approximately 5-15 kDa, selected via the systematic evolution of ligands by exponential enrichment (SELEX) [23,24]. Aptamers are functionally similar to antibodies with high specificity and affinity, which has led to the term "chemical antibody" [25]. They are easy to produce through in vitro chemical synthesis and therefore have little variation between batches, are relatively inexpensive, are usually supplied as stable powders, can be stored for long periods at temperatures of 4•C or even RT, and are therefore more readily available than antibodies stored at ultra-low temperatures [26,27].…”

Section: Introductionmentioning

confidence: 99%

Self-Responsive Fluorescence Aptasensor for Lactoferrin Determination in Dairy Products

Liu,

Gao,

Qin

et al. 2024

Molecules

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In this study, a self-responsive fluorescence aptasensor was established for the determination of lactoferrin (Lf) in dairy products. Herein, the aptamer itself functions as both a recognition element that specifically binds to Lf and a fluorescent signal reporter in conjunction with fluorescent moiety. In the presence of Lf, the aptamer preferentially binds to Lf due to its specific and high-affinity recognition by folding into a self-assembled and three-dimensional spatial structure. Meanwhile, its reduced spatial distance in the aptamer–Lf complex induces a FRET phenomenon based on the quenching of 6-FAM by amino acids in the Lf protein, resulting in a turn-off of the fluorescence of the system. As a result, the Lf concentration can be determined straightforwardly corresponding to the change in the self-responsive fluorescence signal. Under the optimized conditions, good linearities (R2 > 0.99) were achieved in an Lf concentration range of 2~10 μg/mL for both standard solutions and the spiked matrix, as well as with the desirable detection limits of 0.68 μg/mL and 0.46 μg/mL, respectively. Moreover, the fluorescence aptasensor exhibited reliable recoveries (89.5–104.3%) in terms of detecting Lf in three commercial samples, which is comparable to the accuracy of the HPCE method. The fluorescence aptasensor offers a user-friendly, cost-efficient, and promising sensor platform for point-of-need detection.

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Improving aptamer performance: key factors and strategies

Cited by 26 publications

References 122 publications

Oligomeric amyloid-β targeted contrast agent for MRI evaluation of Alzheimer’s disease mouse models

Oligomeric amyloid-β targeted contrast agent for MRI evaluation of Alzheimer’s disease mouse models

A Universal Aptamer for Influenza A Viruses: Selection, Recognition, and Infection Inhibition

Self-Responsive Fluorescence Aptasensor for Lactoferrin Determination in Dairy Products

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