TY - JOUR
T1 - Synthesis and binding analysis of unique AG2 pentasaccharide to human Siglec-2 using NMR techniques
AU - Hanashima, Shinya
AU - Sato, Ken ichi
AU - Naito, Yuko
AU - Takematsu, Hiromu
AU - Kozutsumi, Yasunori
AU - Ito, Yukishige
AU - Yamaguchi, Yoshiki
N1 - Funding Information:
We thank Ms. K. Matsumoto (RIKEN) for preparation of Siglec-2. We thank Dr. S. Akai (Kanagawa University) for helpful discussions. This work was supported by the Science Frontier Project of Kanagawa University and by Grants-in-Aid for Scientific Research for Young Scientists B (No. 20710171 to S.H.) from the Japan Society for the Promotion of Science . Global COE program of Osaka University from the Ministry of Education, Culture, Sports, Science, and Technology of Japan supported this work, in part. We thank Ms. K. Ueno and Ms. I. Hara for technical assistance.
PY - 2010/6/1
Y1 - 2010/6/1
N2 - Siglec-2 is a mammalian sialic acid binding protein expressed on B-cell surfaces and is involved in the modulation of B-cell mediated immune response. We synthesized a unique starfish ganglioside, AG2 pentasaccharide Galfβ(1-3)Galpα(1-4)Neu5Acα(2-3)Galpβ(1-4)Glcp, and found that the synthetic pentasaccharide binds to human Siglec-2 by performing 1H NMR experiments. Saturation transfer difference NMR experiments indicated that the C7-C9 side-chain and the acetamide moiety of the central sialic acid residue were located in the binding face of human Siglec-2. We determined the binding epitope of AG2 pentasaccharide to human Siglec-2, as the Galpα(1-4)Neu5Acα(2-3)Galp unit.
AB - Siglec-2 is a mammalian sialic acid binding protein expressed on B-cell surfaces and is involved in the modulation of B-cell mediated immune response. We synthesized a unique starfish ganglioside, AG2 pentasaccharide Galfβ(1-3)Galpα(1-4)Neu5Acα(2-3)Galpβ(1-4)Glcp, and found that the synthetic pentasaccharide binds to human Siglec-2 by performing 1H NMR experiments. Saturation transfer difference NMR experiments indicated that the C7-C9 side-chain and the acetamide moiety of the central sialic acid residue were located in the binding face of human Siglec-2. We determined the binding epitope of AG2 pentasaccharide to human Siglec-2, as the Galpα(1-4)Neu5Acα(2-3)Galp unit.
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U2 - 10.1016/j.bmc.2010.03.062
DO - 10.1016/j.bmc.2010.03.062
M3 - Article
C2 - 20409718
AN - SCOPUS:77953133153
SN - 0968-0896
VL - 18
SP - 3720
EP - 3725
JO - Bioorganic and Medicinal Chemistry
JF - Bioorganic and Medicinal Chemistry
IS - 11
ER -