Sialic Acid Linkage
Sialic Acid Linkage - Related Videos
12:06
Metabolic Glycoengineering of Sialic Acid Using N-acyl-modified Mannosamines
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Cited by 7 •
2017
Sialic acid is a typical monosaccharide-unit found in glycoconjugates. It is involved in a plethora of molecular and cellular interactions. Here we present a method to modify cell surface sialic acid expression using metabolic glycoengineering with N-acetylmannosamine derivatives.
08:04
Determination of Sialic Acids in Liver and Milk Samples of Wild-type and CMAH Knock-out Mice.
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Cited by 7 •
2017
We describe a HPLC-based method for the determination of N-acetylneuraminic acid and N-glycolylenuraminic acid in mouse liver and milk.
00:49
Ligand Binding and Linkage
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2020
Allosteric proteins have more than one ligand binding site; the binding of a ligand to any of these sites influences the binding of ligands to the other sites. When a protein is allosteric, its binding sites are called coupled or linked. In the case of enzymes, the site that binds to the substrate is known as the active site and the other site is known as the regulatory site. When a ligand binds to the regulatory site, this leads to conformational changes in the protein that can influence the...
03:31
Reversed-Phase High-Performance Liquid Chromatography: A Robust Method for Quantitation of Fluorescently Labeled and Derivatized Sialic Acids Isolated from Mouse Liver
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2025
In this video, we demonstrate the detection of sialic acids, N-acetylneuraminic acid and N-glycolylneuraminic acid, using high-performance liquid chromatography, HPLC, following derivatization with a suitable fluorescent labeling reagent to aid in fluorescence detection.
01:17
Phosphodiester Linkages
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2026
A phosphodiester bond forms when a phosphoric acid molecule (H3PO4) links with two hydroxyl groups (–OH) of two other molecules, forming two ester bonds. Two water molecules are released in this process. The phosphodiester bond is commonly found in nucleic acids (DNA and RNA) and plays a critical role in their structure and function.Phosphodiester Bonds Link Nucleotides TogetherDNA and RNA are polynucleotides or long chains of nucleotides that are linked together. A nucleotide is composed of a...
FAQs
The two configurations present different three-dimensional glycan arrangements and can change how exposed the terminal sialic acid is. Those structural differences influence whether lectins, antibodies, or microbial proteins can bind efficiently. Consequently, glycoconjugates carrying α2-3 rather than α2-6 linkages may support different recognition patterns, helping explain selective cellular interactions during immune responses or infection.
Accessibility determines whether a binding protein can physically reach the terminal sialic acid within a glycoconjugate. Even when sialic acid is present, its position and surrounding glycan shape may limit or facilitate contact with a lectin, antibody, or microbial protein. Linkage analysis therefore provides structural context that simple detection of sialic acid abundance cannot supply.
Microbial proteins, including viral recognition proteins, may interact preferentially with particular glycan arrangements. If α2-3 and α2-6 configurations differ in abundance or accessibility among cell types, those differences can affect where attachment is favored. Studying the pattern of sialic acid linkage can therefore connect receptor recognition with tissue tropism, the tendency of a pathogen to target particular tissues.
Glycan profiling examines patterns across glycoconjugates, whereas linkage-specific probes focus on distinguishing particular sialic acid configurations. Used together, they provide complementary information: profiling reveals the broader glycan landscape, while targeted probes help identify whether α2-3 or α2-6 linkages contribute to a recognition pattern. This combination supports more precise interpretation of cellular and pathogen-binding data.
Researchers compare glycan profiles and apply linkage-specific probes to determine which configurations are present and associated with recognition. The resulting patterns can be evaluated alongside interactions involving lectins, antibodies, or microbial proteins. This workflow helps investigate immune signaling, pathogen attachment, and receptor preferences without treating total sialic acid detection as sufficient evidence of functional equivalence.
Linkage analysis contributes to diagnostics by helping characterize glycan patterns associated with recognition events. In infection research, it supports studies of viral receptor use, pathogen attachment, and tissue tropism. The same structural information can guide vaccine research and improve understanding of immune signaling by showing how alternative glycan configurations shape interactions with cellular or microbial binding partners.