153362-93-7Relevant academic research and scientific papers
Structure of the Complex between a Heparan Sulfate Octasaccharide and Mycobacterial Heparin-Binding Hemagglutinin
Huang, Teng-Yi,Irene, Deli,Zulueta, Medel Manuel L.,Tai, Tzu-Jui,Lain, Shih-Han,Cheng, Cheng-Po,Tsai, Ping-Xi,Lin, Shu-Yi,Chen, Zhi-Geng,Ku, Chiao-Chu,Hsiao, Chwan-Deng,Chyan, Chia-Lin,Hung, Shang-Cheng
, p. 4192 - 4196 (2017)
Heparin-binding hemagglutinin (HBHA) is a 199 amino acid virulence factor at the envelope of Mycobacterium tuberculosis that contributes to latent tuberculosis. The binding of HBHA to respiratory epithelial cells, which leads to extrapulmonary dissemination of the pathogen, is mediated by cell-surface heparan sulfate (HS). We report the structural characterization of the HBHA/HS complex by NMR spectroscopy. To develop a model for the molecular recognition, the first chemically synthesized uniformly 13C- and 15N-labeled HS octasaccharide and a uniformly 13C- and 15N-labeled form of HBHA were prepared. Residues 180–195 at the C-terminal region of HBHA show large chemical shift perturbation upon association with the octasaccharide. Molecular dynamics simulations conforming to the multidimensional NMR data revealed key electrostatic and even hydrophobic interactions between the binding partners that may aid in the development of agents targeting the binding event.
Solid-phase synthesis and 1H and 13C high-resolution magic angle spinning NMR of 13C-labeled resin-bound saccharides
Loening, Nikolaus M.,Kanemitsu, Takuya,Seeberger, Peter H.,Griffin, Robert G.
, p. 453 - 458 (2007/10/03)
We show how high-resolution magic angle-spinning NMR spectroscopy can be used to characterize 13C-labeled saccharides that have been prepared using solid-phase synthesis techniques while they are still bound to a solid-support resin. With the u
