Sialic Acid Modification
Sialic Acid Modification - 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.
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.
11:41
Crystallization of Salicylic Acid via Chemical Modification
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2023
Source: Kerry M. Dooley and Michael G. Benton, Department of Chemical Engineering, Louisiana State University, Baton Rouge, LA Processing of biochemicals involves unit operations such as crystallization, ultracentrifugation, membrane filtration, and preparative chromatography, all of which have in common the need to separate large from small molecules, or solid from liquid. Of these, crystallization is the most important from a tonnage standpoint. For that reason, it is commonly employed in the...
02:32
Histone Modification
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2020
The histone proteins have a flexible N-terminal tail extending out from the nucleosome. These histone tails are often subjected to post-translational modifications such as acetylation, methylation, phosphorylation, and ubiquitination. Particular combinations of these modifications form “histone codes” that influence the chromatin folding and tissue-specific gene expression. Acetylation The enzyme histone acetyltransferase adds acetyl group to the histones. Another enzyme, histone deacetylase,...
FAQs
Sialyltransferases add sialic acid residues to glycans, whereas sialidases remove them. This opposing enzymatic control allows researchers to increase or decrease terminal sialylation on glycoproteins and cell-surface structures. The choice of enzyme determines whether the engineered system gains or loses specific terminal sugars, enabling deliberate adjustment of glycan composition rather than uncontrolled alteration.
Terminal sialylation influences several properties at the glycan surface, including molecular recognition, charge, stability, and interactions with cells. Altering these residues can therefore change how a glycoprotein, biomaterial, or engineered cell system is perceived by surrounding biological components. This makes sialic acid modification useful for investigating signaling and for designing systems with selected interaction profiles.
Metabolic and chemical engineering provide alternatives to directly adding or removing residues with purified enzymes. Metabolic strategies alter the cellular pathways that produce or use sialic acid, while chemical approaches modify sialic acid-related structures through controlled chemical alteration. Together, these methods expand the ways bioengineers can adjust glycan composition in cells and engineered materials.
The appropriate direction depends on the desired glycan composition and resulting biological behavior. Addition through sialyltransferases may increase terminal sialylation, while removal through sialidases may expose a less-sialylated glycan pattern. Researchers can select either strategy when they need to examine or engineer changes in recognition, stability, charge, or cell interactions.
A general approach begins by identifying the desired change in glycan composition and selecting an enzymatic, metabolic, or chemical strategy. Researchers then apply that strategy to a glycoprotein, biomaterial, or engineered cell system and examine the resulting functional properties. The workflow connects molecular alteration with outcomes such as stability, recognition, charge, or cellular interaction.
Controlled modification can support the design of biopharmaceuticals, targeted delivery platforms, biomaterials, and engineered cell systems. In each case, adjusting terminal sialylation provides a way to tune how the resulting construct behaves in relation to molecules or cells. The approach is especially relevant when glycan composition affects stability, recognition, or biological targeting.
Engineered changes in sialic acid patterns create experimental systems in which researchers can examine how glycan features influence cellular recognition and communication. Such systems can help connect specific changes in terminal sialylation with cell signaling behavior or interactions between host cells and pathogens. This provides bioengineering tools for studying mechanisms as well as building controlled model systems.