Molecular Recognition of Sialic Acid End Groups by Phenylboronates

2005 ◽  
Vol 11 (13) ◽  
pp. 4010-4018 ◽  
Author(s):  
Kristina Djanashvili ◽  
Luca Frullano ◽  
Joop A. Peters
Keyword(s):  
Sialic Acid ◽  
Molecular Recognition ◽  
End Groups

scholarly journals Sialic Acid-Responsive Polymeric Interface Material: From Molecular Recognition to Macroscopic Property Switching

2017 ◽  
Vol 7 (1) ◽  
Author(s):  
Yuting Xiong ◽  
Ge Jiang ◽  
Minmin Li ◽  
Guangyan Qing ◽  
Xiuling Li ◽  
...  
Keyword(s):  
Sialic Acid ◽  
Molecular Recognition ◽  
Macroscopic Property

Molecular Recognition of Sialic Acid by Lanthanide(III) Complexes through Cooperative Two-Site Binding

2010 ◽  
Vol 49 (9) ◽  
pp. 4212-4223 ◽  
Author(s):  
Martín Regueiro-Figueroa ◽  
Kristina Djanashvili ◽  
David Esteban-Gómez ◽  
Thomas Chauvin ◽  
Éva Tóth ◽  
...  
Keyword(s):  
Sialic Acid ◽  
Molecular Recognition ◽  
Site Binding

The conformation of end-groups is one determinant of carotenoid topology suitable for high fidelity molecular recognition: A study of β- and ε-end-groups

2010 ◽  
Vol 493 (2) ◽  
pp. 169-174 ◽  
Author(s):  
John T. Landrum ◽  
David C. Chatfield ◽  
Alex M. Mebel ◽  
Francesca Alvarez-Calderon ◽  
Melissa V. Fernandez
Keyword(s):  
Molecular Recognition ◽  
High Fidelity ◽  
End Groups

scholarly journals The structure of a glycopeptide purified from porcine thyroglobulin

1971 ◽  
Vol 123 (3) ◽  
pp. 415-420 ◽  
Author(s):  
Minoru Fukuda ◽  
Fujio Egami
Keyword(s):  
Sialic Acid ◽  
Sodium Borohydride ◽  
Periodate Oxidation ◽  
Galactose Oxidase ◽  
Borohydride Reduction ◽  
Enzymic Hydrolysis ◽  
End Groups ◽  
Sodium Borohydride Reduction

1. The structure of a purified glycopeptide isolated from porcine thyroglobulin was studied by sequential hydrolysis with specific glycosidases, by periodate oxidation and by treatment with galactose oxidase. 2. Sequential hydrolysis with several combinations of neuraminidase, α-l-fucosidase, β-d-galactosidase, β-N-acetyl-d-glucosaminidase and α-d-mannosidase presented the evidence for the following structure. 3. The monosaccharide sequence of the peripheral moiety of the heteropolysaccharide chain was sialic acid→galactose→N-acetylglucosamine. Some of the galactose residues were non-reducing end-groups with the sequence galactose→N-acetylglucosamine. 4. After removal of the peripheral moiety composed of sialic acid, fucose, galactose and N-acetylglucosamine, α-mannosidase released 1.4mol of mannose/mol of glycopeptide, indicating that two of the three mannose residues were located between peripheral N-acetylglucosamine and internal N-acetylglucosamine or mannose. 5. Periodate oxidation and sodium borohydride reduction confirmed the results obtained by enzymic degradation and gave information concerning the position of substitution. 6. Based on the results obtained by enzymic hydrolysis and periodate oxidation together with the treatment with galactose oxidase, a structure is proposed for the glycopeptide.

Improved procedures for the conjugation of oligosaccharides to protein by reductive amination

1984 ◽  
Vol 62 (5) ◽  
pp. 270-275 ◽  
Author(s):  
René Roy ◽  
Ewa Katzenellenbogen ◽  
Harold J. Jennings
Keyword(s):  
Sialic Acid ◽  
Bovine Serum Albumin ◽  
Bovine Serum ◽  
Reductive Amination ◽  
Reaction Model ◽  
Model Studies ◽  
End Groups ◽  
Coupling Procedure ◽  
Lysine Residues ◽  
Optimized Conditions

The rate of coupling of oligosaccharides having aldose end groups to protein by reductive amination was significantly increased by changing the temperature and pH of the reaction, and even more significantly by the addition of borate ions. Under optimized conditions half of the lysine residues of bovine serum albumin could be derivatized by lactose in 7 h and their complete derivatization was achieved in approximately 24 h. All attempts to carry out similar reductive amination procedures using oligosaccharides having ketose (D-fructose, 3-deoxy-D-manno-octulosonic acid (KDO), and sialic acid) failed owing to the slowness of the reaction. Model studies on the coupling of D-fructose and KDO to glycine indicate that any coupling procedure based on reductive amination of ketose residues would of necessity require the prior introduction of a small functionalized spacer molecule.

scholarly journals Group B Streptococcal Type II and III Conjugate Vaccines: Physicochemical Properties That Influence Immunogenicity

2006 ◽  
Vol 13 (8) ◽  
pp. 936-943 ◽  
Author(s):  
Francis Michon ◽  
Catherine Uitz ◽  
Arun Sarkar ◽  
Anello J. D'Ambra ◽  
Maryline Laude-Sharp ◽  
...  
Keyword(s):  
Sialic Acid ◽  
Reductive Amination ◽  
High Titer ◽  
Type Ii ◽  
Group B Streptococci ◽  
End Groups ◽  
Group B ◽  
Aldehyde Groups ◽  
Opsonophagocytic Killing ◽  
Acid Labile

ABSTRACT Recent efforts toward developing vaccines against group B streptococci (GBS) have focused on increasing the immunogenicity of GBS polysaccharides by conjugation to carrier proteins. However, partial depolymerization of GBS polysaccharides for the production of vaccines is a difficult task because of their acid-labile, antigenically critical sialic acids. Here we report a method for the partial depolymerization of type II and III polysaccharides by mild deaminative cleavage to antigenic fragments with reducing-terminal 2,5-anhydro-d-mannose residues. Through the free aldehydes of their newly formed end groups, the fragments were conjugated to tetanus toxoid by reductive amination. The resulting conjugates stimulated the production in animals of high-titer type II- and III-specific antibodies which induced opsonophagocytic killing of type II and III strains of group B streptococci. For the type II conjugates, immunogenicity increased as oligosaccharide size decreased, whereas for type III conjugates, the size of the oligosaccharides did not significantly influence immunogenicity. When oligosaccharides of defined size were conjugated through sialic acid residues, the resulting cross-linkages were shown to affect immunogenicity. When oligosaccharides were conjugated through terminal aldehyde groups generated by deamination, modification of the exocyclic chain of sialic acid did not influence immunogenicity.

Synthesis and labelling of a phenylboranate derivative with 68Ga for molecular recognition of overexpressed sialic acid on tumor cells

2019 ◽  
Vol 72-73 ◽  
pp. S40
Author(s):  
A. Shegani ◽  
M. Kaplanis ◽  
C. Kiritsis ◽  
M. Ischyropoulou ◽  
M. Vlastara ◽  
...  
Keyword(s):  
Sialic Acid ◽  
Molecular Recognition ◽  
Tumor Cells

scholarly journals Molecular Recognition Insights of Sialic Acid Glycans by Distinct Receptors Unveiled by NMR and Molecular Modeling

2021 ◽  
Vol 8 ◽  
Author(s):  
Cátia Oliveira Soares ◽  
Ana Sofia Grosso ◽  
June Ereño-Orbea ◽  
Helena Coelho ◽  
Filipa Marcelo
Keyword(s):  
Sialic Acid ◽  
Molecular Modeling ◽  
Nmr Spectroscopy ◽  
Molecular Recognition ◽  
Complex Structure ◽  
Structural Features ◽  
Sialic Acids ◽  
Infection Process ◽  
Human Cells ◽  
Host Cells

All cells are decorated with a highly dense and complex structure of glycan chains, which are mostly attached to proteins and lipids. In this context, sialic acids are a family of nine-carbon acidic monosaccharides typically found at the terminal position of glycan chains, modulating several physiological and pathological processes. Sialic acids have many structural and modulatory roles due to their negative charge and hydrophilicity. In addition, the recognition of sialic acid glycans by mammalian cell lectins, such as siglecs, has been described as an important immunological checkpoint. Furthermore, sialic acid glycans also play a pivotal role in host–pathogen interactions. Various pathogen receptors exposed on the surface of viruses and bacteria are responsible for the binding to sialic acid sugars located on the surface of host cells, becoming a critical point of contact in the infection process. Understanding the molecular mechanism of sialic acid glycans recognition by sialic acid-binding proteins, present on the surface of pathogens or human cells, is essential to realize the biological mechanism of these events and paves the way for the rational development of strategies to modulate sialic acid-protein interactions in diseases. In this perspective, nuclear magnetic resonance (NMR) spectroscopy, assisted with molecular modeling protocols, is a versatile and powerful technique to investigate the structural and dynamic aspects of glycoconjugates and their interactions in solution at the atomic level. NMR provides the corresponding ligand and protein epitopes, essential for designing and developing potential glycan-based therapies. In this review, we critically discuss the current state of knowledge about the structural features behind the molecular recognition of sialic acid glycans by different receptors, naturally present on human cells or pathogens, disclosed by NMR spectroscopy and molecular modeling protocols.

scholarly journals Molecular recognition of sialoglycans by streptococcal Siglec-like adhesins: toward the shape of specific inhibitors

2021 ◽  
Author(s):  
Cristina Di Carluccio ◽  
Alba Silipo ◽  
Roberta Marchetti ◽  
Barbara Ben ◽  
Koichi Fukase ◽  
...  
Keyword(s):  
Sialic Acid ◽  
Infective Endocarditis ◽  
Molecular Recognition ◽  
Oral Cavity ◽  
Commensal Bacteria ◽  
Streptococcus Gordonii ◽  
Healthy Individuals ◽  
Sialic Acid Binding ◽  
Specific Inhibitors

Streptococcus gordonii and sanguinis, commensal bacteria present in the oral cavity of healthy individuals, upon entry into the bloodstream can become pathogenic, causing infective endocarditis (IE). Sialic acid-binding serine-rich repeat...

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