Abstract
Syndecan-4 cytoplasmic domain was tested to confirm the interactions with the bilayer membrane using <TEX>$^{31}P$</TEX> solid-state NMR measurements. Syndecan-4 was known as a coreceptor with integrins in the cell adhesion. The syndecan-4 V region is not understood of its functional roles and tested its ability of the interaction with multilamellar vesicles. The <TEX>$^{31}P$</TEX> powder pattern was dramatically changed and showed isotropic peak which imply the bilayer membrane changed its topology to the micelle-like structure. Especially, phosphatidylcholine membrane was affected this effect more than phosphatidylethanolamine membrane.
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