Chemically Defined Sialoside Scaffolds for Investigation of Multivalent Interactions with Sialic Acid Binding Proteins†

2003 ◽  
Vol 68 (22) ◽  
pp. 8485-8493 ◽  
Author(s):  
Stacey A. Kalovidouris ◽  
Ola Blixt ◽  
Alshakim Nelson ◽  
Sébastien Vidal ◽  
W. Bruce Turnbull ◽  
...  
Keyword(s):  
Sialic Acid ◽  
Binding Proteins ◽  
Sialic Acid Binding ◽  
Multivalent Interactions

Modulation of sialic acid-binding proteins of rat uterus in response to changing hormonal milieu

1993 ◽  
Vol 126 (1) ◽  
pp. 77-86 ◽  
Author(s):  
Indrani Chakraborty ◽  
Chhabinath Mandal ◽  
Mridula Chowdhury
Keyword(s):  
Sialic Acid ◽  
Binding Proteins ◽  
Rat Uterus ◽  
Sialic Acid Binding ◽  
Hormonal Milieu

scholarly journals Siglec Ligands

Cells ◽  
2021 ◽  
Vol 10 (5) ◽  
pp. 1260
Author(s):  
Anabel Gonzalez-Gil ◽  
Ronald L. Schnaar
Keyword(s):  
Immune System ◽  
Sialic Acid ◽  
Therapeutic Intervention ◽  
Binding Proteins ◽  
Cellular Responses ◽  
Cell Physiology ◽  
Molecular Pathways ◽  
Cell Surfaces ◽  
Sugar Moiety ◽  
Sialic Acid Binding

A dense and diverse array of glycans on glycoproteins and glycolipids decorate all cell surfaces. In vertebrates, many of these carry sialic acid, in a variety of linkages and glycan contexts, as their outermost sugar moiety. Among their functions, glycans engage complementary glycan binding proteins (lectins) to regulate cell physiology. Among the glycan binding proteins are the Siglecs, sialic acid binding immunoglobulin-like lectins. In humans, there are 14 Siglecs, most of which are expressed on overlapping subsets of immune system cells. Each Siglec engages distinct, endogenous sialylated glycans that initiate signaling programs and regulate cellular responses. Here, we explore the emerging science of Siglec ligands, including endogenous sialoglycoproteins and glycolipids and synthetic sialomimetics. Knowledge in this field promises to reveal new molecular pathways controlling cell physiology and new opportunities for therapeutic intervention.

scholarly journals A Glycal-Based Photoaffinity Probe That Enriches Sialic Acid Binding Proteins

2019 ◽  
Author(s):  
Peter Thuy-Boun ◽  
Dennis Wolan
Keyword(s):  
Sialic Acid ◽  
Binding Proteins ◽  
Binding Protein ◽  
Factor H ◽  
Protein Profiling ◽  
Complement Factor ◽  
Acid Binding Protein ◽  
Sialic Acid Binding ◽  
Kinetic Inhibition ◽  
Protein Complement

<p>To identify sialic acid binding proteins from complex proteomes, three photocrosslinking affinity-based probes were constructed using Neu5Ac (<b>5 </b>and <b>6</b>) and Neu5Ac2en (<b>7</b>) scaffolds. Kinetic inhibition assays and Western blotting revealed the Neu5Ac2en-based <b>7 </b>to be an effective probe for the labeling of a purified gut microbial sialidase (BDI_2946) and a purified human sialic acid binding protein (hCD33). Additionally, LC-MS/MS affinity-based protein profiling verified the ability of <b>7</b>to enrich a low-abundance sialic acid binding protein (complement factor H) from human serum thus validating the utility of this probe in a complex context.</p>

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