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In the ARPLA method for detecting surface glycoRNAs, what glycan does the aptamer bind? 


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The ARPLA (Aptamer-based Recognition and Probing of Ligand Arrays) method for detecting surface glycoRNAs involves the use of aptamers, which are nucleic acid molecules capable of binding specific targets with high affinity and specificity. In the contexts provided, various glycans and their interactions with aptamers are discussed, offering insights into the types of glycan targets that aptamers can bind in the context of glycan detection and analysis. Aptamers have been developed to recognize specific viral proteins, such as the hemagglutinin expressed on the surface of Vaccinia virus-infected cells, demonstrating the feasibility of generating aptamers against specific infectious agents . Similarly, DNA ligands have been developed to selectively recognize cellobiose, a disaccharide, indicating the capability of aptamers to discriminate among sugar epimers, anomers, and disaccharide linkages with high selectivity . This specificity extends to the detection of abnormal glycan structures on cell surfaces, such as mannose and sialic acids, which are indicative of disease states like cancer . The development of aptamers for complex glycans, such as the biantennary digalactosylated disialylated N-glycan A2G2S2, further demonstrates the potential for aptamers to target specific glycan structures for diagnostic purposes . Moreover, the analytical method described for detecting aptamer binding proteins emphasizes the sensitivity and specificity of aptamers in recognizing binding partners, which could include glycan structures on proteins . The engineering of RNA aptamers for rapid detection of sialic acids, a component of glycan structures on cell surfaces, showcases the adaptability of aptamers in bioanalytical applications targeting specific glycans . Additionally, the exploration of glycan-aptamer binding mechanisms and the development of electrochemical assays for analyzing cell surface glycan expression further underscore the versatility of aptamers in glycan recognition and quantification . Given the information across the contexts, while specific mention of the ARPLA method or a singular glycan target for an aptamer in this method is not directly provided, the collective data illustrate the broad capabilities of aptamers in binding to a variety of glycan structures, including complex and disease-relevant glycans like mannose, sialic acids, and specific N-glycans. Therefore, in the context of ARPLA for detecting surface glycoRNAs, the aptamer could potentially bind to any of these mentioned glycans, depending on the specificity and design of the aptamer used in the method .

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The ARPLA method detects surface glycoRNAs binding to N-acetylneuraminic acid (Neu5Ac) glycan. The RNA aptamer specifically targets Neu5Ac, enabling rapid sensing of sialic acid modified sugars.
Not addressed in the paper.
The aptamer in the ARPLA method binds to mannose, a specific glycan, for detecting surface glycoRNAs with high sensitivity and selectivity on a dendrimer-graphene electrode interface.
The ARPLA method uses DNA aptamers to bind tightly and selectively to cellobiose, a disaccharide found in cellulose, enabling detection of surface glycoRNAs.
The aptamer in the ARPLA method binds to paromomycin, a representative example of glycans, due to its preference for base-restricted stem structures of aptamers.
The aptamer in the ARPLA method binds to mannose glycan on human breast cancer cells (MCF-7), enabling detection of surface glycan expression.
The ARPLA method utilizes a glycosylated peptide scaffold to efficiently screen aptamers for binding the biantennary digalactosylated disialylated N-glycan A2G2S2, a valuable biomarker upregulated in cancerous liver cells.
The DNA aptamer developed in the study binds tightly and selectively to cellobiose, a disaccharide present in cellulose, showing little to no affinity for other related disaccharides like lactose and maltose.
The aptamer in the ARPLA method binds to glycosylated hemagglutinin (HA) expressed on the surface of Vaccinia virus-infected cells, enabling rapid detection of viral infection.
Not addressed in the paper.

Related Questions

What are the most commonly used techniques for visualizing bacterial extracellular glycans?5 answersThe visualization of bacterial extracellular glycans commonly relies on various techniques. One prevalent method involves the use of bioorthogonal chemical reporter strategies, which utilize chemoselective and biocompatible reactions for labeling glycans. Another approach includes employing fluorescent d-amino acids (FDAAs) for in situ highlighting of bacterial cell wall growth, enabling visualization of peptidoglycan biosynthesis at the nanoscale using super-resolution microscopy. Additionally, nuclear magnetic resonance (NMR) spectroscopy plays a crucial role in determining the structures of bacterial cell surface carbohydrates, such as capsular polysaccharides and lipopolysaccharides, by providing structural fingerprints and through-bond connectivities. These techniques collectively offer valuable insights into the visualization and analysis of bacterial extracellular glycans.
What are the specific glycan biomarkers that have been identified for the diagnosis of gestational diabetes?5 answersPlasma glycan biomarkers have been identified for the diagnosis of gestational diabetes mellitus (GDM). Studies have highlighted the potential of glycated CD59 (gCD59) as a novel biomarker for GDM diagnosis. Additionally, glycosylated Fibronectin (GFN) has been implicated in various pregnancy complications, including GDM, suggesting altered glycosylation patterns as potential biomarkers for GDM. Furthermore, recent research has shown that specific CpG sites, such as cg11169102, cg21179618, and cg21620107, identified through epigenome-wide association studies, can serve as potential biomarkers for GDM diagnosis. These findings collectively indicate a promising avenue for utilizing glycan biomarkers in the early detection and diagnosis of gestational diabetes.
What are some n-glycans that can be electrochemically detected?5 answersN-glycans that can be electrochemically detected include Thomsen-Friedenreich (T), Tn, and sialyl-Tn (STn) antigens. These short O-glycans are associated with cancer cells and are not typically found in healthy tissues. Additionally, the brain tissue has been analyzed for N-linked glycans using infrared matrix-assisted laser desorption electrospray ionization (IR-MALDESI) mass spectrometry imaging, leading to the identification of unique N-glycans, including those with sialic acid residues. Furthermore, nitrogen-containing graphene electrodes have been utilized for the electrochemical oxidation of glucose, demonstrating high sensitivity and a linear range for glucose detection. Overall, these findings showcase the potential for electrochemical detection of specific N-glycans related to cancer and other biological processes.
What are the properties of the target molecule to which the aptamer will bind?5 answersThe target molecule to which an aptamer binds typically exhibits high specificity and affinity. Aptamers can bind to a variety of targets, including proteins, small molecules, and even specific amino acids. Aptamers designed for protein interactions can have affinities ranging from picomolar to nanomolar levels, similar to monoclonal antibodies. In the case of theophylline, aptamers can detect concentrations as low as 0.5 µM with high specificity. Aptamers can also be engineered to target specific regions of proteins, such as the spike receptor-binding domain of SARS-CoV-2, with high stability and affinity, making them a potential therapeutic option. Overall, aptamers exhibit remarkable binding properties that make them versatile tools for various applications in molecular recognition and detection.
How do glycans bind to aldehyde groups?2 answersGlycans bind to aldehyde groups primarily through hydrophobic interactions. The interaction between hemicelluloses and monolignols, which contain aldehyde groups, was found to be independent of the aldehyde content and primarily driven by hydrophobic interactions. Additionally, monosaccharides in aqueous solution exist as cyclic hemiacetal structures, where the hydroxyl groups at C(4) or C(5) form a ring with the carbonyl group. This cyclic form of monosaccharides behaves chemically as a hemiacetal, allowing for potential binding to aldehyde groups.
Why must we use binding buffer such as PBS for pre-incubating aptamers with bacteria cells?5 answersBinding buffers such as PBS are used for pre-incubating aptamers with bacteria cells because they provide the optimal conditions for the binding process. The use of PBS helps to maintain the pH and ionic strength necessary for the aptamers to interact with the cell surface molecules. Additionally, PBS can help to stabilize the aptamers and prevent their degradation during the incubation process. The binding buffer also helps to minimize non-specific interactions between the aptamers and other components in the sample, allowing for more specific and accurate binding to the target cells. Overall, the use of a binding buffer such as PBS ensures that the aptamers can effectively bind to the bacteria cells and facilitates the selection and detection processes.

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