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Book ; Online: Marine Glycomics

Fujii, Yuki / Gerdol, Marco / Ozeki, Yasuhiro

2022

Keywords	Research & information: general ; Biology, life sciences ; Acropora tenuis ; coral ; chemoattraction ; lectin ; white-spotted charr lectin ; oncolytic vaccinia virus ; interferon ; antiviral response ; Chlorella vulgaris ; Dunaliella salina ; Arthrospira platensis ; growth rate ; accumulation of carbohydrates ; biohydrogen ; antibacterial activity ; anticancer activity ; antifungal activity ; Aplysia kurodai ; apoptosis ; Ehrlich ascites carcinoma ; sulfated fucose-rich polysaccharides ; sulfated fucan ; fucosylated chondroitin sulfate ; fucoidan ; oral administration ; anticoagulant activity ; fucosylated glycosaminoglycan ; anticoagulant ; platelet aggregation ; contact activation ; hypotension ; pulmonary embolism ; sulfated polysaccharides ; marine hydrobionts ; antiparasitic activity ; protozoa ; malaria ; leishmaniasis ; trypanosomiasis ; schistosomiasis ; cryptosporidiosis ; trichomoniasis ; bivalve mollusk ; C1q domain-containing ; lectin-like ; pattern recognition receptor ; polysaccharides ; interstitial compartment ; marine worms ; sipunculids ; bioactive properties ; peptides ; rotifera ; pattern recognition receptors ; microbe-associated molecular patterns ; innate immunity ; C-type lectins ; C1q domain-containing proteins ; galectins ; bacterial exopolysaccharides ; bioflocculanting activity ; microalgae growth-promoting bacterium ; harmful algal bloom-forming dinoflagellate ; Alexandrium catenella ; Mameliella alba ; n/a
Language	English
Size	1 electronic resource (208 pages)
Publisher	MDPI - Multidisciplinary Digital Publishing Institute
Publishing place	Basel
Document type	Book ; Online
Note	English
HBZ-ID	HT030380099
ISBN	9783036558226 ; 3036558225
Database	ZB MED Catalogue: Medicine, Health, Nutrition, Environment, Agriculture

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Book ; Online: Marine Glycobiology, Glycomics and Lectins

Ozeki, Yasuhiro

2019

Abstract: Glycans (carbohydrate chains) of marine creatures are rich and diverse in polysaccharides, glycoproteins, and glycolipids. The chains that are metabolized by glycan-related enzymes (glycosyltransferases and glycosidases) are recognized by glycan-binding ... ...

Abstract	Glycans (carbohydrate chains) of marine creatures are rich and diverse in polysaccharides, glycoproteins, and glycolipids. The chains that are metabolized by glycan-related enzymes (glycosyltransferases and glycosidases) are recognized by glycan-binding proteins (lectins) which regulate cellular processes such as growth, differentiation, and death. Marine glycomics that involves the genome and transcriptome accelerates our understanding of the evolution of glycans, glycan-related enzymes, and lectins. From 2017 to 2019, the Special Issue "Marine Glycobiology, Glycomics and Lectins" of the journal Marine Drugs published scientific articles and reviews, on the background of "glycobiology"-that is, glycan-based biosciences. The aim was to promote the discovery of novel biomolecules that contribute to drug development and clinical studies. This has great potential for establishing connections between the fields of both human health and marine life sciences.This book contains 11 scientific papers representing current topics in comprehensive glycosciences related to therapeutic agents from marine natural products, as outlined
Keywords	Science (General) ; Biology (General) ; Biochemistry
Size	1 electronic resource (176 pages)
Publisher	MDPI - Multidisciplinary Digital Publishing Institute
Document type	Book ; Online
Note	eng ; Open Access
HBZ-ID	HT020324172
ISBN	9783039218202 ; 9783039218219 ; 3039218204 ; 3039218212
DOI	10.3390/books978-3-03921-821-9
Database	ZB MED Catalogue: Medicine, Health, Nutrition, Environment, Agriculture

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Article ; Online: Flavonoids as potential KRAS inhibitors: DFT, molecular docking, molecular dynamics simulation and ADMET analyses.

Prinsa / Saha, Supriyo / Bulbul, Md Zahidul Haque / Ozeki, Yasuhiro / Alamri, Mubarak A / Kawsar, Sarkar M A

Journal of Asian natural products research

2024 , Page(s) 1–38

Abstract: KRAS mutations linked with cancer. Flavonoids were docked against KRAS G12C and G12D receptors. Abyssinone III, alpha naphthoflavone, beta naphthoflavone, abyssinone I, abyssinone II and beta naphthoflavone, genistin, daidzin showed good docking scores ... ...

Abstract	KRAS mutations linked with cancer. Flavonoids were docked against KRAS G12C and G12D receptors. Abyssinone III, alpha naphthoflavone, beta naphthoflavone, abyssinone I, abyssinone II and beta naphthoflavone, genistin, daidzin showed good docking scores against KRAS G12C and G12D receptors, respectively. The MD simulation data revealed that Rg, RMSD, RMSF, and SASA values were within acceptable limits. Alpha and beta naphthoflavone showed good binding energies with KRAS G12C and G12D receptors. DFT and MEP analysis highlighted the nucleophilic and electrophilic zones of best-docked flavonoids. A novel avenue for the control of KRAS G12C and G12D mutations is made possible by flavonoids.
Language	English
Publishing date	2024-04-22
Publishing country	England
Document type	Journal Article
ZDB-ID	2077926-4
ISSN	1477-2213 ; 1028-6020
ISSN (online)	1477-2213
ISSN	1028-6020
DOI	10.1080/10286020.2024.2343821
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Article ; Online: In Silico Pharmacokinetics, Molecular Docking and Molecular Dynamics Simulation Studies of Nucleoside Analogs for Drug Discovery- A Mini Review.

Kawsar, Sarkar M A / Munia, Nasrin S / Saha, Supriyo / Ozeki, Yasuhiro

Mini reviews in medicinal chemistry

2023

Abstract: Nucleoside analogs have been widely used as antiviral, antitumor, and antiparasitic agents due to their ability to inhibit nucleic acid synthesis. Adenosine, cytidine, guanosine, thymidine and uridine analogs such as didanosine, vidarabine, remdesivir, ... ...

Abstract	Nucleoside analogs have been widely used as antiviral, antitumor, and antiparasitic agents due to their ability to inhibit nucleic acid synthesis. Adenosine, cytidine, guanosine, thymidine and uridine analogs such as didanosine, vidarabine, remdesivir, gemcitabine, lamivudine, acyclovir, abacavir, zidovusine, stavudine, and idoxuridine showed remarkable anticancer and antiviral activities. In our previously published articles, our main intention was to develop newer generation nucleoside analogs with acylation-induced modification of the hydroxyl group and showcase their biological potencies. In the process of developing nucleoside analogs, in silico studies play an important role and provide a scientific background for biological data. Molecular interactions between drugs and receptors followed by assessment of their stability in physiological environments, help to optimize the drug development process and minimize the burden of unwanted synthesis. Computational approaches, such as DFT, FMO, MEP, ADMET prediction, PASS prediction, POM analysis, molecular docking, and molecular dynamics simulation, are the most popular tools to culminate all preclinical study data and deliver a molecule with maximum bioactivity and minimum toxicity. Although clinical drug trials are crucial for providing dosage recommendations, they can only indirectly provide mechanistic information through researchers for pathological, physiological, and pharmacological determinants. As a result, in silico approaches are increasingly used in drug discovery and development to provide mechanistic information of clinical value. This article portrays the current status of these methods and highlights some remarkable contributions to the development of nucleoside analogs with optimized bioactivity.
Language	English
Publishing date	2023-11-10
Publishing country	Netherlands
Document type	Journal Article
ZDB-ID	2104081-3
ISSN	1875-5607 ; 1389-5575
ISSN (online)	1875-5607
ISSN	1389-5575
DOI	10.2174/0113895575258033231024073521
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Article ; Online: Coming New Age of Marine Glycomics: The Fundamental, Medical, and Ecological Aspects.

Fujii, Yuki / Gerdol, Marco / Ozeki, Yasuhiro

Marine drugs

2022 Volume 20, Issue 10

Abstract: This Special Issue "Marine Glycomics" (https://www.mdpi.com/journal/marinedrugs/special_issues/Marine_Glycomics, accessed on 12 September 2022) provided new approachesand information on bioactive compounds, such as glycans and lectins from marine animals, ...

Abstract	This Special Issue "Marine Glycomics" (https://www.mdpi.com/journal/marinedrugs/special_issues/Marine_Glycomics, accessed on 12 September 2022) provided new approachesand information on bioactive compounds, such as glycans and lectins from marine animals,seaweeds, and microorganisms for the application of clinical therapy and elucidation of thephysiological functions of marine organisms [...].
MeSH term(s)	Animals ; Glycomics ; Lectins ; Polysaccharides ; Aquatic Organisms
Chemical Substances	Lectins ; Polysaccharides
Language	English
Publishing date	2022-09-28
Publishing country	Switzerland
Document type	Editorial
ZDB-ID	2175190-0
ISSN	1660-3397 ; 1660-3397
ISSN (online)	1660-3397
ISSN	1660-3397
DOI	10.3390/md20100613
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Article ; Online: Histochemical localization of N-acetylhexosamine-binding lectin HOL-18 in Halichondria okadai (Japanese black sponge), and its antimicrobial and cytotoxic anticancer effects.

Hasan, Imtiaj / Ozeki, Yasuhiro

International journal of biological macromolecules

2018 Volume 124, Page(s) 819–827

Abstract: We studied localization and physiological activities of a lectin showing specific binding to N-acetylhexosamines, termed HOL-18, purified from Japanese black sponge (Halichondria okadai). Antiserum against the lectin was generated in rabbit and applied ... ...

Abstract	We studied localization and physiological activities of a lectin showing specific binding to N-acetylhexosamines, termed HOL-18, purified from Japanese black sponge (Halichondria okadai). Antiserum against the lectin was generated in rabbit and applied for immunohistochemical analyses. HOL-18 was expressed specifically around water pores and on spicules of sponge tissues. It showed strong binding to a variety of N-acetylhexosamines: N-acetyl D-glucosamine, N-acetyl D-galactosamine, N-acetyl mannosamine, N-acetyl muramic acid, and N-acetyl neuraminic acid. Hemagglutination induced by the lectin was inhibited by lipopolysaccharides and a peptidoglycan. HOL-18 inhibited growth of a gram-positive bacterium (Listeria monocytogenes), gram-negative bacteria (Escherichia coli, Shigella boydii, Pseudomonas aeruginosa), and a fungus (Aspergillus niger). It displayed anti-biofilm activity against P. aeruginosa. HOL-18 was internalized into conidiophores of A. niger, and displayed notable antifungal activity. Fluorescence microscopy revealed binding and incorporation of the lectin into human cancer cell lines HeLa, MCF-7, and T47D, but not Caco-2. HOL-18 displayed dose-dependent cytotoxic effects against HeLa, MCF-7, and T47D, with respective IC
MeSH term(s)	Animals ; Anti-Infective Agents/chemistry ; Anti-Infective Agents/isolation & purification ; Anti-Infective Agents/metabolism ; Anti-Infective Agents/pharmacology ; Antineoplastic Agents/chemistry ; Antineoplastic Agents/isolation & purification ; Antineoplastic Agents/metabolism ; Antineoplastic Agents/pharmacology ; Aspergillus niger/drug effects ; Aspergillus niger/growth & development ; Biofilms/drug effects ; Biofilms/growth & development ; Caspase 3/genetics ; Caspase 3/metabolism ; Escherichia coli/drug effects ; Escherichia coli/growth & development ; HeLa Cells ; Hemagglutination Tests ; Hexosamines/chemistry ; Hexosamines/metabolism ; Humans ; Lectins/chemistry ; Lectins/isolation & purification ; Lectins/metabolism ; Lectins/pharmacology ; Lipopolysaccharides/pharmacology ; Listeria monocytogenes/drug effects ; Listeria monocytogenes/growth & development ; MCF-7 Cells ; Microbial Sensitivity Tests ; Mitogen-Activated Protein Kinase 1/genetics ; Mitogen-Activated Protein Kinase 1/metabolism ; Mitogen-Activated Protein Kinase 3/genetics ; Mitogen-Activated Protein Kinase 3/metabolism ; Peptidoglycan/pharmacology ; Phosphorylation/drug effects ; Porifera/chemistry ; Protein Binding ; Pseudomonas aeruginosa/drug effects ; Pseudomonas aeruginosa/growth & development ; Rabbits ; Shigella boydii/drug effects ; Shigella boydii/growth & development
Chemical Substances	Anti-Infective Agents ; Antineoplastic Agents ; Hexosamines ; Lectins ; Lipopolysaccharides ; Peptidoglycan ; MAPK1 protein, human (EC 2.7.11.24) ; MAPK3 protein, human (EC 2.7.11.24) ; Mitogen-Activated Protein Kinase 1 (EC 2.7.11.24) ; Mitogen-Activated Protein Kinase 3 (EC 2.7.11.24) ; CASP3 protein, human (EC 3.4.22.-) ; Caspase 3 (EC 3.4.22.-)
Language	English
Publishing date	2018-11-26
Publishing country	Netherlands
Document type	Journal Article
ZDB-ID	282732-3
ISSN	1879-0003 ; 0141-8130
ISSN (online)	1879-0003
ISSN	0141-8130
DOI	10.1016/j.ijbiomac.2018.11.222
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Article ; Online: Physicochemical properties and antimicrobial activities of MytiLec-1, a member from the mytilectin family of mussels.

Hossain, Md Mikail / Rajia, Sultana / Ohkawa, Mayuka / Yoshimoto, Suzuna / Fujii, Yuki / Kawsar, Sarkar M A / Ozeki, Yasuhiro / Hasan, Imtiaj

International journal of biological macromolecules

2023 Volume 253, Issue Pt 8, Page(s) 127628

Abstract: MytiLec-1, the recombinant form of a mussel lectin from Mytillus galloprovincialis, was purified by affinity chromatography and showed the maximum hemagglutination activity at a temperature range of 10 °C to 40 °C and at pH 7.0 to 9.0. Denaturants like ... ...

Abstract	MytiLec-1, the recombinant form of a mussel lectin from Mytillus galloprovincialis, was purified by affinity chromatography and showed the maximum hemagglutination activity at a temperature range of 10 °C to 40 °C and at pH 7.0 to 9.0. Denaturants like urea and acidic-guanidine inhibited its hemagglutination activity significantly. MytiLec-1 was found to be metal-independent though Ca
MeSH term(s)	Animals ; Lectins/chemistry ; Mytilus/chemistry ; Disaccharides/metabolism ; Anti-Infective Agents/pharmacology ; Anti-Infective Agents/metabolism
Chemical Substances	MytiLec-1 ; Lectins ; Disaccharides ; Anti-Infective Agents
Language	English
Publishing date	2023-10-24
Publishing country	Netherlands
Document type	Journal Article
ZDB-ID	282732-3
ISSN	1879-0003 ; 0141-8130
ISSN (online)	1879-0003
ISSN	0141-8130
DOI	10.1016/j.ijbiomac.2023.127628
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Article ; Online: Taxonomic Distribution and Molecular Evolution of Mytilectins.

Gerdol, Marco / Nerelli, Daniela Eugenia / Martelossi, Nicola / Ogawa, Yukiko / Fujii, Yuki / Pallavicini, Alberto / Ozeki, Yasuhiro

Marine drugs

2023 Volume 21, Issue 12

Abstract: R-type lectins are a widespread group of sugar-binding proteins found in nearly all domains of life, characterized by the presence of a carbohydrate-binding domain that adopts a β-trefoil fold. Mytilectins represent a recently described subgroup of β- ... ...

Abstract	R-type lectins are a widespread group of sugar-binding proteins found in nearly all domains of life, characterized by the presence of a carbohydrate-binding domain that adopts a β-trefoil fold. Mytilectins represent a recently described subgroup of β-trefoil lectins, which have been functionally characterized in a few mussel species (Mollusca, Bivalvia) and display attractive properties, which may fuel the development of artificial lectins with different biotechnological applications. The detection of different paralogous genes in mussels, together with the description of orthologous sequences in brachiopods, supports the formal description of mytilectins as a gene family. However, to date, an investigation of the taxonomic distribution of these lectins and their molecular diversification and evolution was still lacking. Here, we provide a comprehensive overview of the evolutionary history of mytilectins, revealing an ancient monophyletic evolutionary origin and a very broad but highly discontinuous taxonomic distribution, ranging from heteroscleromorphan sponges to ophiuroid and crinoid echinoderms. Moreover, the overwhelming majority of mytilectins display a chimera-like architecture, which combines the β-trefoil carbohydrate recognition domain with a C-terminal pore-forming domain, suggesting that the simpler structure of most functionally characterized mytilectins derives from a secondary domain loss.
MeSH term(s)	Animals ; Lectins/chemistry ; Evolution, Molecular ; Bivalvia/metabolism ; Carbohydrates/genetics
Chemical Substances	Lectins ; Carbohydrates
Language	English
Publishing date	2023-11-27
Publishing country	Switzerland
Document type	Review ; Journal Article
ZDB-ID	2175190-0
ISSN	1660-3397 ; 1660-3397
ISSN (online)	1660-3397
ISSN	1660-3397
DOI	10.3390/md21120614
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Article: Macromolecules: Synthesis, antimicrobial, POM analysis and computational approaches of some glucoside derivatives bearing acyl moieties.

Kayes, Mohammad R / Saha, Supriyo / Alanazi, Mohammed M / Ozeki, Yasuhiro / Pal, Dilipkumar / Hadda, Taibi B / Legssyer, Abdelkhaleq / Kawsar, Sarkar M A

Saudi pharmaceutical journal : SPJ : the official publication of the Saudi Pharmaceutical Society

2023 Volume 31, Issue 11, Page(s) 101804

Abstract: Macromolecules i.e., carbohydrate derivatives are crucial to biochemical and medical research. Herein, we designed and synthesized eight methyl α-D-glucopyranoside (MGP) derivatives ( ...

Abstract	Macromolecules i.e., carbohydrate derivatives are crucial to biochemical and medical research. Herein, we designed and synthesized eight methyl α-D-glucopyranoside (MGP) derivatives (
Language	English
Publishing date	2023-10-02
Publishing country	Saudi Arabia
Document type	Journal Article
ZDB-ID	1378024-4
ISSN	1319-0164
ISSN	1319-0164
DOI	10.1016/j.jsps.2023.101804
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Article ; Online: Functional Characterization of OXYL, A SghC1qDC LacNAc-specific Lectin from The Crinoid Feather Star

Hasan, Imtiaj / Gerdol, Marco / Fujii, Yuki / Ozeki, Yasuhiro

Marine drugs

2019 Volume 17, Issue 2

Abstract: We identified a lectin (carbohydrate-binding protein) belonging to the complement 1q(C1q) family in the feather ... ...

Abstract	We identified a lectin (carbohydrate-binding protein) belonging to the complement 1q(C1q) family in the feather star
MeSH term(s)	Agglutination/drug effects ; Amino Acid Sequence ; Amino Sugars/chemistry ; Amino Sugars/metabolism ; Animals ; Base Sequence ; Biofilms/drug effects ; Caspase 3/metabolism ; Cell Line, Tumor ; Echinodermata/chemistry ; Humans ; Lectins/chemistry ; Lectins/genetics ; Lectins/metabolism ; Lectins/pharmacology ; Protein Binding ; Pseudomonas aeruginosa/drug effects ; p38 Mitogen-Activated Protein Kinases/metabolism
Chemical Substances	Amino Sugars ; Lectins ; N-acetyllactosamine (3Y5B2K5OOK) ; p38 Mitogen-Activated Protein Kinases (EC 2.7.11.24) ; Caspase 3 (EC 3.4.22.-)
Language	English
Publishing date	2019-02-25
Publishing country	Switzerland
Document type	Journal Article
ZDB-ID	2175190-0
ISSN	1660-3397 ; 1660-3397
ISSN (online)	1660-3397
ISSN	1660-3397
DOI	10.3390/md17020136
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