The Chemistry Department is located in the Merkert Chemistry Center, a 109,000 square foot structure designed to empower the dynamic, cutting-edge research for which the department is internationally recognized. The Merkert Chemistry Center contains faculty research laboratories in organic chemistry, chemical biology, and physical chemistry; specialized research facilities and shared instrumentation; and classrooms and teaching laboratories.
08.24.2020 Masayuki Wasa: Direct Conversion of N-Alkylamines to N-Propargylamines through C–H Activation Promoted by Lewis Acid/Organocopper Catalysis: Application to Late-Stage Functionalization of Bioactive Molecules
07.15.2019 Dunwei Wang: Electrochemical CO2 reduction
08.01.2018 Masayuki Wasa: C–H Functionalization of Amines via Alkene-Derived Nucleophiles through Cooperative Action of Chiral and Achiral Lewis Acid Catalysts: Applications in Enantioselective Synthesis
“Clickable Disaccharides” Lead to Efficient Assembly of Glycomimetics
Udayan Mohanty and Jia Niu
February 27, 2023
Cell surface glycans play important roles in a variety of cell functions ranging from signaling transduction to cell-pathogen interactions to cancer development. However, understanding of the structures and functions of cell surface glycans has been hampered by their highly heterogenous structure and modifications. Recently Professors Jia Niu and Udayan Mohanty, postdoc Cangjie Yang, and graduate students Yu Deng and Yang Wang teamed up to tackle this challenge. They developed a facile approach to generating glycomimetics with complex sulfation patterns through iterative assembly of clickable disaccharide building blocks that mimic the disaccharide repeating units of heparan sulfate, a type of highly sulfated cell surface glycan. The team demonstrated that assembly of variably sulfated clickable disaccharides can facilely generate a library of mass spec-sequenceable glycomimetic oligomers with defined sulfation patterns by solution-phase iterative syntheses. Molecular dynamics (MD) simulations further confirmed that these glycomimetic oligomers bind protein fibroblast growth factor 2 (FGF2) in a sulfation-dependent manner consistent with that of the native glycans. This work established a general approach to glycomimetics that can potentially serve as alternatives to native glycans in both fundamental research and disease models.