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Monolayers assembled from a glycolipid biosurfactant from <Emphasis Type="Italic">Pseudozyma</Emphasis> (<Emphasis Type="Italic">Candida</Emphasis>) <Emphasis Type="Italic">antarctica</Emphasis> serve as a high-affinity ligand system for immunoglobulin G and M |
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| Authors: | Tomohiro Imura Seya Ito Reiko Azumi Hiroshi Yanagishita Hideki Sakai Masahiko Abe Dai Kitamoto |
| Institution: | (1) Research Institute for Innovation in Sustainable Chemistry, National Institute of Advanced Industrial Science and Technology (AIST), Tsukuba Central 5-2, 1-1-1 Higashi, Tsukuba, Ibaraki 305-8565, Japan;(2) Faculty of Science and Technology, Tokyo University of Science, 2641 Yamazaki, Noda, Chiba 278-8510, Japan;(3) Photonics Research Institute, National Institute of Advanced Industrial Science and Technology (AIST), Tsukuba Central 5-1, 1-1-1 Higashi, Ibaraki 305-8565, Japan |
| Abstract: | A carbohydrate ligand system has been developed which is composed of self-assembled monolayers (SAMs) of mannosylerythritol lipid-A (MEL-A) from Pseudozyma antarctica, serving for human immunoglobulin G and M (HIgG and HIgM). The estimated binding constants from surface plasmon resonance (SPR) measurement were K a = 9.4 × 106 M−1 for HIgG and 5.4 × 106 M−1 for HIgM, respectively. The binding site was not in the Fc region of immunoglobulin but in the Fab region. Large amounts of HIgG and HIgM bound to MEL-A SAMs were directly observed by atomic force microscopy. |
| Keywords: | Atomic force microscopy Biosurfactant Immunoglobulin Protein-carbohydrate interaction Surface plasmon resonance |
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