Abstract
Mannosylerythritol lipids (MEL), which are glycolipid biosurfactants secreted by the Pseudozyma yeasts, show not only excellent surface-active properties but also versatile biochemical actions including antitumor and cell-differentiation activities. In order to address the biochemical actions, interactions between MEL-A, the major component of MEL, and different lectins were investigated using the surface plasmon resonance spectroscopy. The monolayer of MEL-A showed high binding affinity to concanavalin A (ConA) and Maackia amurensis lectin-I (MAL-I). The observed affinity constants for ConA and MAL-I were estimated to be 9.48 ± 1.31 × 106 and 3.13 ± 0.274 × 106 M−1, respectively; the value was comparable to that of Manα1–6(Manα1–3)Man, which is one of the most specific probe to ConA. Significantly, α-methyl-D-mannopyranoside (1 mM) exhibited no binding inhibition between MEL-A and ConA. MEL-A is thus likely to self-assemble to give a high affinity surface, where ConA binds to the hydrophilic headgroup in a different manner from that generally observed in lectin-saccharide interactions. The binding manner should be related with the biochemical actions of MEL toward mammalian cells via protein-carbohydrate interactions.






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Acknowledgement
We wish to thank Mr. S. Itoh of Tokyo University of Science for his kind instruction on SPR study. We also would like to thank Ms. A. Sugimura, a fellow of the Japan Industrial Technology Association, for her technical assistance. This work was supported by the Industrial Technology Research Grant Program in 05A33008c from the New Energy and Industrial Technology Development Organization (NEDO) of Japan.
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Konishi, M., Imura, T., Fukuoka, T. et al. A yeast glycolipid biosurfactant, mannosylerythritol lipid, shows high binding affinity towards lectins on a self-assembled monolayer system. Biotechnol Lett 29, 473–480 (2007). https://doi.org/10.1007/s10529-006-9261-x
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DOI: https://doi.org/10.1007/s10529-006-9261-x