title: Exploring the Binding Proteins of Glycolipids with Bifunctional Chemical Probes.
abstract: Glycolipids are important structural components of biological membranes and perform crucial functions in living systems, including signaling transduction and interaction with extracellular environment. However, the mechanistic exploration of glycolipids in vivo is challenging because they are not genetically encoded. Herein, we designed and synthesized a series of bifunctional monogalactosyldiacylglycerol (MGDG) probes as a model by introducing diazirine and terminal alkyne moieties on an aliphatic chain. In combination with proteome profiling and molecular modeling, we have demonstrated that MGDG alleviates inflammation by antagonizing TLR4.
authors.affiliation: School of Pharmaceutical Science and Technology, Tianjin University, Tianjin, 300072, China.
authors.forename: Xiaohui
authors.initials: X
authors.lastname: Liu
authors.affiliation: Beijing National Laboratory for Molecular Sciences, Key Laboratory of Bioorganic Chemistry and Molecular Engineering of Ministry of Education, Department of Chemical Biology, College of Chemistry and Molecular Engineering, Synthetic and Functional Biomolecules Center, and Peking-Tsinghua Center for Life Sciences, Peking University, Beijing, 100871, China.
authors.forename: Ting
authors.initials: T
authors.lastname: Dong
authors.affiliation: National Institute of Biological Sciences (NIBS), Changping District, Beijing, 102206, China.
authors.forename: Yu
authors.initials: Y
authors.lastname: Zhou
authors.affiliation: National Institute of Biological Sciences (NIBS), Changping District, Beijing, 102206, China.
authors.forename: Niu
authors.initials: N
authors.lastname: Huang
authors.affiliation: Beijing National Laboratory for Molecular Sciences, Key Laboratory of Bioorganic Chemistry and Molecular Engineering of Ministry of Education, Department of Chemical Biology, College of Chemistry and Molecular Engineering, Synthetic and Functional Biomolecules Center, and Peking-Tsinghua Center for Life Sciences, Peking University, Beijing, 100871, China. xglei@pku.edu.cn.
authors.forename: Xiaoguang
authors.initials: X
authors.lastname: Lei
mesh_terms: D000480:Alkynes / Q000737:chemistry; D019902:Chondrocytes / Q000166:cytology / Q000187:drug effects / Q000378:metabolism; D057930:Click Chemistry; D003978:Diazomethane / Q000737:chemistry; D004591:Electrophoresis, Polyacrylamide Gel; D038983:Galactolipids / Q000737:chemistry* / Q000494:pharmacology; D006017:Glycolipids / Q000737:chemistry*; D006801:Humans; D051218:Lymphocyte Antigen 96 / Q000737:chemistry / Q000378:metabolism; D013058:Mass Spectrometry; D011506:Proteins / Q000737:chemistry* / Q000378:metabolism; D051197:Toll-Like Receptor 4 / Q000737:chemistry / Q000378:metabolism; D014466:Ultraviolet Rays
chemical_list: D000480:Alkynes; D038983:Galactolipids; D006017:Glycolipids; C495377:LY96 protein, human; D051218:Lymphocyte Antigen 96; D011506:Proteins; D051197:Toll-Like Receptor 4; C009909:monogalactosyldiacylglycerol; D003978:Diazomethane
keywords: click chemistry; glycolipids; minimalist linker; photoaffinity labeling; target identification