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Book: Macro-glycoligands

Sun, Xue-Long

(Methods in molecular biology ; 1367 ; Springer protocols)

2016

Author's details	edited by Xue-Long Sun
Series title	Methods in molecular biology ; 1367 Springer protocols
Collection
Keywords	Polymers/Biotechnology
Subject code	668.9
Language	English
Size	XIII, 226 S. : Ill., graph. Darst., 26 cm
Publisher	Humana Press
Publishing place	New York u.a.
Publishing country	United States
Document type	Book
HBZ-ID	HT018816543
ISBN	978-1-4939-3129-3 ; 978-1-4939-3130-9 ; 1-4939-3129-6 ; 1-4939-3130-X
Database	Catalogue ZB MED Medicine, Health

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Article ; Online: The role of cell surface sialic acids for SARS-CoV-2 infection.

Sun, Xue-Long

Glycobiology

2021 Volume 31, Issue 10, Page(s) 1245–1253

Abstract: Severe acute respiratory syndrome coronavirus-2 (SARS-CoV-2) is a new virus that has higher contagious capacity than any other previous human coronaviruses (HCoVs) and causes the current coronavirus disease 2019 pandemic. Sialic acids are a group of nine- ...

Abstract	Severe acute respiratory syndrome coronavirus-2 (SARS-CoV-2) is a new virus that has higher contagious capacity than any other previous human coronaviruses (HCoVs) and causes the current coronavirus disease 2019 pandemic. Sialic acids are a group of nine-carbon acidic α-keto sugars, usually located at the end of glycans of cell surface glycoconjugates and serve as attachment sites for previous HCoVs. It is therefore speculated that sialic acids on the host cell surface could serve as co-receptors or attachment factors for SARS-CoV-2 cell entry as well. Recent in silico modeling, molecular modeling predictions and microscopy studies indicate potential sialic acid binding by SARS-CoV-2 upon cell entry. In particular, a flat sialic acid-binding domain was proposed at the N-terminal domain of the spike protein, which may lead to the initial contact and interaction of the virus on the epithelium followed by higher affinity binding to angiotensin-converting enzyme 2 (ACE2) receptor, likely a two-step attachment fashion. However, recent in vitro and ex vivo studies of sialic acids on ACE2 receptor confirmed an opposite role for SARS-CoV-2 binding. In particular, neuraminidase treatment of epithelial cells and ACE2-expressing 293T cells increased SARS-CoV-2 binding. Furthermore, the ACE2 glycosylation inhibition studies indicate that sialic acids on ACE2 receptor prevent ACE2-spike protein interaction. On the other hand, a most recent study indicates that gangliosides could serve as ligands for receptor-binding domain of SARS-CoV-2 spike protein. This mini-review discusses what has been predicted and known so far about the role of sialic acid for SARS-CoV-2 infection and future research perspective.
MeSH term(s)	Binding Sites ; COVID-19/epidemiology ; COVID-19/metabolism ; COVID-19/virology ; Cell Membrane/metabolism ; Glycosylation ; Humans ; Protein Binding ; Receptors, Virus/metabolism ; SARS-CoV-2/isolation & purification ; SARS-CoV-2/metabolism ; Sialic Acids/metabolism
Chemical Substances	Receptors, Virus ; Sialic Acids
Language	English
Publishing date	2021-04-27
Publishing country	England
Document type	Journal Article ; Research Support, N.I.H., Extramural ; Review
ZDB-ID	1067689-2
ISSN	1460-2423 ; 0959-6658
ISSN (online)	1460-2423
ISSN	0959-6658
DOI	10.1093/glycob/cwab032
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Article ; Online: Solvent Isotope Effects on the Creation of Fluorescent Quantum Defects in Carbon Nanotubes by Aryl Diazonium Chemistry.

Heppe, Brandon J / Dzombic, Nina / Keil, Joseph M / Sun, Xue-Long / Ao, Geyou

Journal of the American Chemical Society

2023 Volume 145, Issue 47, Page(s) 25621–25631

Abstract: The integration of aryl diazonium and carbon nanotube chemistries has offered rich and versatile tools for creating nanomaterials of unique optical and electronic properties in a controllable fashion. The diazonium reaction with single-wall carbon ... ...

Abstract	The integration of aryl diazonium and carbon nanotube chemistries has offered rich and versatile tools for creating nanomaterials of unique optical and electronic properties in a controllable fashion. The diazonium reaction with single-wall carbon nanotubes (SWCNTs) is known to proceed through a radical or carbocation mechanism in aqueous solutions, with deuterated water (D
Language	English
Publishing date	2023-11-16
Publishing country	United States
Document type	Journal Article
ZDB-ID	3155-0
ISSN	1520-5126 ; 0002-7863
ISSN (online)	1520-5126
ISSN	0002-7863
DOI	10.1021/jacs.3c07341
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Article ; Online: Investigation of cofactor activities of endothelial microparticle-thrombomodulin with liposomal surrogate

Gruzdys, Valentinas / Wang, Lin / Wang, Dan / Huang, Rachel / Sun, Xue-Long

Biochemical and Biophysical Research Communications.

2023

Abstract: Thrombomodulin (TM) is a type I transmembrane glycoprotein mainly expressed on the endothelial cells, where it binds thrombin to form the thrombin-TM complex that can activate protein C and thrombin-activable fibrinolysis inhibitor (TAFI) and induce ... ...

Abstract	Thrombomodulin (TM) is a type I transmembrane glycoprotein mainly expressed on the endothelial cells, where it binds thrombin to form the thrombin-TM complex that can activate protein C and thrombin-activable fibrinolysis inhibitor (TAFI) and induce anticoagulant and anti-fibrinolytic reactions, respectively. Cell activation and injury often sheds microparticles that contain membrane TM, which circulate in biofluids like blood. However, the biological function of circulating microparticle-TM is still unknown even though it has been recognized as biomarker of endothelial cell injury and damage. In comparison with cell membrane, different phospholipids are exposed on the microparticle surface due to cell membrane ''flip-flop'' upon cell activation and injury. Liposomes can be used as a microparticle mimetics. In this report, we prepared TM-containing liposomes with different phospholipids as surrogates of endothelial microparticle-TM and investigated their cofactor activities. We found that liposomal TM with phosphatidylethanolamine (PtEtn) showed increased protein C activation but decreased TAFI activation in comparison to liposomal TM with phosphatidylcholine (PtCho). In addition, we investigated whether protein C and TAFI compete for the thrombin/TM complex on the liposomes. We found that protein C and TAFI did not compete for the thrombin/TM complex on the liposomes with PtCho alone and with low concentration (5%) of PtEtn and phosphatidylserine (PtSer), but competed each other on the liposomes with higher concentration (10%) of PtEtn and PtSer. These results indicate that membrane lipids affect protein C and TAFI activation and microparticle-TM may have different cofactor activities in comparison to cell membrane TM.
Keywords	anticoagulants ; biomarkers ; blood ; cell membranes ; endothelial cells ; fibrinolysis ; glycoproteins ; microparticles ; phosphatidylcholines ; phosphatidylethanolamines ; phosphatidylserines ; research ; thrombin ; Thrombomodulin ; Microparticle ; Protein C ; TAFI ; Hemostasis ; Phospholipids ; Liposomes
Language	English
Publishing place	Elsevier Inc.
Document type	Article ; Online
Note	Pre-press version
ZDB-ID	205723-2
ISSN	0006-291X ; 0006-291X
ISSN (online)	0006-291X
ISSN	0006-291X
DOI	10.1016/j.bbrc.2023.02.024
Database	NAL-Catalogue (AGRICOLA)

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Article ; Online: Investigation of cofactor activities of endothelial microparticle-thrombomodulin with liposomal surrogate.

Gruzdys, Valentinas / Wang, Lin / Wang, Dan / Huang, Rachel / Sun, Xue-Long

Biochemical and biophysical research communications

2023 Volume 651, Page(s) 79–84

Abstract	Thrombomodulin (TM) is a type I transmembrane glycoprotein mainly expressed on the endothelial cells, where it binds thrombin to form the thrombin-TM complex that can activate protein C and thrombin-activable fibrinolysis inhibitor (TAFI) and induce anticoagulant and anti-fibrinolytic reactions, respectively. Cell activation and injury often sheds microparticles that contain membrane TM, which circulate in biofluids like blood. However, the biological function of circulating microparticle-TM is still unknown even though it has been recognized as a biomarker of endothelial cell injury and damage. In comparison with cell membrane, different phospholipids are exposed on the microparticle surface due to cell membrane ''flip-flop'' upon cell activation and injury. Liposomes can be used as a microparticle mimetics. In this report, we prepared TM-containing liposomes with different phospholipids as surrogates of endothelial microparticle-TM and investigated their cofactor activities. We found that liposomal TM with phosphatidylethanolamine (PtEtn) showed increased protein C activation but decreased TAFI activation in comparison to liposomal TM with phosphatidylcholine (PtCho). In addition, we investigated whether protein C and TAFI compete for the thrombin/TM complex on the liposomes. We found that protein C and TAFI did not compete for the thrombin/TM complex on the liposomes with PtCho alone and with low concentration (5%) of PtEtn and phosphatidylserine (PtSer), but competed each other on the liposomes with higher concentration (10%) of PtEtn and PtSer. These results indicate that membrane lipids affect protein C and TAFI activation and microparticle-TM may have different cofactor activities in comparison to cell membrane TM.
MeSH term(s)	Protein C/metabolism ; Thrombin/metabolism ; Endothelial Cells/metabolism ; Thrombomodulin/metabolism ; Liposomes ; Fibrinolysis
Chemical Substances	Protein C ; Thrombin (EC 3.4.21.5) ; Thrombomodulin ; Liposomes
Language	English
Publishing date	2023-02-10
Publishing country	United States
Document type	Journal Article ; Research Support, U.S. Gov't, Non-P.H.S. ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't
ZDB-ID	205723-2
ISSN	1090-2104 ; 0006-291X ; 0006-291X
ISSN (online)	1090-2104 ; 0006-291X
ISSN	0006-291X
DOI	10.1016/j.bbrc.2023.02.024
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Article ; Online: Circulating Thrombomodulin: Release Mechanisms, Measurements, and Levels in Diseases and Medical Procedures.

Boron, Mallorie / Hauzer-Martin, Tiffany / Keil, Joseph / Sun, Xue-Long

TH open : companion journal to thrombosis and haemostasis

2022 Volume 6, Issue 3, Page(s) e194–e212

Abstract: Thrombomodulin (TM) is a type-I transmembrane protein that is mainly expressed on endothelial cells and plays important roles in many biological processes. Circulating TM of different forms are also present in biofluids, such as blood and urine. Soluble ... ...

Abstract	Thrombomodulin (TM) is a type-I transmembrane protein that is mainly expressed on endothelial cells and plays important roles in many biological processes. Circulating TM of different forms are also present in biofluids, such as blood and urine. Soluble TM (sTM), comprised of several domains of TM, is the major circulating TM which is generated by either enzymatic or chemical cleavage of the intact protein under different conditions. Under normal conditions, sTM is present in low concentrations (<10 ng/mL) in the blood but is elevated in several pathological conditions associated with endothelial dysfunction such as cardiovascular, inflammatory, infection, and metabolic diseases. Therefore, sTM level has been examined for monitoring disease development, such as disseminated intravascular coagulation (DIC), sepsis and multiple organ dysfunction syndrome in patients with novel coronavirus disease 2019 (COVID-19) recently. In addition, microvesicles (MVs) that contain membrane TM (MV-TM) have been found to be released from activated cells which also contribute to levels of circulating TM in certain diseases. Several release mechanisms of sTM and MV-TM have been reported, including enzymatic, chemical, and TM mutation mechanisms. Measurements of sTM and MV-TM have been developed and explored as biomarkers in many diseases. In this review, we summarize all these advances in three categories as follows: (1) release mechanisms of circulating TM, (2) methods for measuring circulating TM in biological samples, and (3) correlation of circulating TM with diseases. Altogether, it provides a whole picture of recent advances on circulating TM in health and disease.
Language	English
Publishing date	2022-07-11
Publishing country	Germany
Document type	Journal Article ; Review
ZDB-ID	2901738-5
ISSN	2512-9465 ; 2567-3459
ISSN (online)	2512-9465
ISSN	2567-3459
DOI	10.1055/a-1801-2055
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Article ; Online: Investigation of substrate specificity of sialidases with membrane mimetic glycoconjugates.

Tomar, Sonia / Sun, Xue-Long

Glycoconjugate journal

2019 Volume 37, Issue 2, Page(s) 175–185

Abstract: Sialidases or neuraminidases play important roles in various physiological and pathological processes by cleaving terminal sialic acids (Sias) (desialylation) from the glycans of both glycoproteins and glycolipids. To understand the biological ... ...

Abstract	Sialidases or neuraminidases play important roles in various physiological and pathological processes by cleaving terminal sialic acids (Sias) (desialylation) from the glycans of both glycoproteins and glycolipids. To understand the biological significance of desialylation by sialidases, it is important to investigate enzyme specificity with native substrate in biological membrane of cells. Herein, we report a membrane-mimicking system with liposome ganglioside conjugates containing different lipids for evaluating substrate specificity of sialidase and the lipid effect on the enzyme activity. Briefly, liposomes of phosphatidylcholine (PC) and cholesterol with ganglioside (GM3 or GM1) along with different percentage of phosphatidylserine (PS) or phosphatidylethanolamine (PE) were prepared and characterized. Their desialylation profiles with Arthrobacter ureafaciens (bacterial) sialidase and H1N1 (influenza viral) sialidase were quantified by HPLC method. A diversity of substrate preference was found for both bacterial and viral sialidase to the liposome ganglioside conjugate platform. The apparent K
MeSH term(s)	Bacterial Proteins/chemistry ; Bacterial Proteins/metabolism ; Cholesterol/chemistry ; Glycoconjugates/chemistry ; Glycoconjugates/metabolism ; Influenza A Virus, H1N1 Subtype/enzymology ; Liposomes/chemistry ; Micrococcaceae/enzymology ; Neuraminidase/chemistry ; Neuraminidase/metabolism ; Phosphatidylcholines/chemistry ; Phosphatidylethanolamines/chemistry ; Phosphatidylserines/chemistry ; Substrate Specificity ; Viral Proteins/chemistry ; Viral Proteins/metabolism
Chemical Substances	Bacterial Proteins ; Glycoconjugates ; Liposomes ; Phosphatidylcholines ; Phosphatidylethanolamines ; Phosphatidylserines ; Viral Proteins ; phosphatidylethanolamine (39382-08-6) ; Cholesterol (97C5T2UQ7J) ; Neuraminidase (EC 3.2.1.18)
Language	English
Publishing date	2019-12-04
Publishing country	United States
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	283770-5
ISSN	1573-4986 ; 0282-0080
ISSN (online)	1573-4986
ISSN	0282-0080
DOI	10.1007/s10719-019-09895-x
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Book: Macro-glycoligands

Sun, Xue-Long

methods and protocols

(Methods in molecular biology, ; 1367 ; Springer protocols,)

2016

Author's details	edited by Xue-Long Sun
Series title	Methods in molecular biology, ; 1367 Springer protocols,
MeSH term(s)	Polymers ; Carbohydrates ; Polymerization ; Nanotechnology
Language	English
Dates of publication	2016-2016
Size	xiii, 226 pages :, illustrations (some color) ;, 26 cm
Document type	Book
ISBN	9781493931293 ; 1493931296 ; 9781493931309 ; 149393130X
Database	Catalogue of the US National Library of Medicine (NLM)

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Article ; Online: Glycopolymer-Wrapped Carbon Nanotubes Show Distinct Interaction of Carbohydrates With Lectins

Ana M. DiLillo / Ka Keung Chan / Xue-Long Sun / Geyou Ao

Frontiers in Chemistry, Vol

2022 Volume 10

Abstract: Glyconanomaterials with unique nanoscale property and carbohydrate functionality show vast potential in biological and biomedical applications. We investigated the interactions of noncovalent complexes of single-wall carbon nanotubes that are wrapped by ... ...

Abstract	Glyconanomaterials with unique nanoscale property and carbohydrate functionality show vast potential in biological and biomedical applications. We investigated the interactions of noncovalent complexes of single-wall carbon nanotubes that are wrapped by disaccharide lactose-containing glycopolymers with the specific carbohydrate-binding proteins. The terminal galactose (Gal) of glycopolymers binds to the specific lectin as expected. Interestingly, an increased aggregation of nanotubes was also observed when interacting with a glucose (Glc) specific lectin, likely due to the removal of Glc groups from the surface of nanotubes resulting from the potential binding of the lectin to the Glc in the glycopolymers. This result indicates that the wrapping conformation of glycopolymers on the surface of nanotubes potentially allows improved accessibility of the Glc for specific lectins. Furthermore, it shows that the interaction between Glc groups in the glycopolymers and nanotubes play a key role in stabilizing the nanocomplexes. Overall, our results demonstrate that nanostructures can enable conformation-dependent interactions of glycopolymers and proteins and can potentially lead to the creation of versatile optical sensors for detecting carbohydrate-protein interactions with enhanced specificity and sensitivity.
Keywords	carbon nanotubes ; glycopolymers ; wrapping conformation ; protein interactions ; optical sensing ; Chemistry ; QD1-999
Language	English
Publishing date	2022-03-01T00:00:00Z
Publisher	Frontiers Media S.A.
Document type	Article ; Online
Database	BASE - Bielefeld Academic Search Engine (life sciences selection)

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Article ; Online: Sialidase substrates for Sialdiase assays - activity, specificity, quantification and inhibition.

Yuan, Lei / Zhao, Yu / Sun, Xue-Long

Glycoconjugate journal

2020 Volume 37, Issue 5, Page(s) 513–531

Abstract: Sialidases are glycosidases responsible for the removal of sialic acid (Sia) residues (desialylation) from glycan portions of either glycoproteins or glycolipids. By desialylation, sialidases are able to modulate the functionality and stability of the ... ...

Abstract	Sialidases are glycosidases responsible for the removal of sialic acid (Sia) residues (desialylation) from glycan portions of either glycoproteins or glycolipids. By desialylation, sialidases are able to modulate the functionality and stability of the Sia-containing molecules and are involved in both physiological and pathological pathways. Therefore, evaluation of sialidase activity and specificity is important for understanding the biological significance of desialylation by sialidases and its function and the related molecular mechanisms of the physiological and pathological pathways. In addition, it is essential for developing novel mechanisms and approaches for disease treatment and diagnosis and pathogen detection as well. This review summarizes the most recent sialidase substrates for evaluating sialidase activity and specificity and screening sialidase inhibitors, including (i) general sialidase substrates, (ii) specific sialidase substrates, (iii) native sialidase substrates and (iv) cellular sialidase substrates. This review also provides a brief introduction of recent instrumental methods for quantifying the sialidase activity, such as UV, fluorescence, HPLC and LC-MS methods.
MeSH term(s)	Enzyme Inhibitors/pharmacology ; Glycoproteins/chemistry ; Glycoproteins/genetics ; Humans ; Neuraminidase/antagonists & inhibitors ; Neuraminidase/chemistry ; Neuraminidase/genetics ; Polysaccharides/chemistry ; Polysaccharides/genetics ; Sialic Acids/chemistry ; Substrate Specificity
Chemical Substances	Enzyme Inhibitors ; Glycoproteins ; Polysaccharides ; Sialic Acids ; Neuraminidase (EC 3.2.1.18)
Language	English
Publishing date	2020-08-19
Publishing country	United States
Document type	Journal Article ; Research Support, Non-U.S. Gov't ; Review
ZDB-ID	283770-5
ISSN	1573-4986 ; 0282-0080
ISSN (online)	1573-4986
ISSN	0282-0080
DOI	10.1007/s10719-020-09940-0
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