Effects of various spacers between biotin and the phospholipid headgroup on immobilization and sedimentation of biotinylated phospholipid-containing liposomes facilitated by avidin-biotin interactions
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作者:
Sakamoto, Yasuhisa
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Kumamoto Univ, Grad Sch Med Sci, Dept Mol Pharmacol, 1-1-1 Honjo, Kumamoto 8608556, JapanKumamoto Univ, Grad Sch Med Sci, Dept Mol Pharmacol, 1-1-1 Honjo, Kumamoto 8608556, Japan
Sakamoto, Yasuhisa
[1
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Kikuchi, Koji
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Kumamoto Univ, Grad Sch Med Sci, Dept Mol Pharmacol, 1-1-1 Honjo, Kumamoto 8608556, JapanKumamoto Univ, Grad Sch Med Sci, Dept Mol Pharmacol, 1-1-1 Honjo, Kumamoto 8608556, Japan
Kikuchi, Koji
[1
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Umeda, Kazuaki
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Kumamoto Univ, Grad Sch Med Sci, Dept Mol Pharmacol, 1-1-1 Honjo, Kumamoto 8608556, JapanKumamoto Univ, Grad Sch Med Sci, Dept Mol Pharmacol, 1-1-1 Honjo, Kumamoto 8608556, Japan
Umeda, Kazuaki
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]
Nakanishi, Hiroyuki
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Kumamoto Univ, Grad Sch Med Sci, Dept Mol Pharmacol, 1-1-1 Honjo, Kumamoto 8608556, JapanKumamoto Univ, Grad Sch Med Sci, Dept Mol Pharmacol, 1-1-1 Honjo, Kumamoto 8608556, Japan
Nakanishi, Hiroyuki
[1
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机构:
[1] Kumamoto Univ, Grad Sch Med Sci, Dept Mol Pharmacol, 1-1-1 Honjo, Kumamoto 8608556, Japan
Immobilization and sedimentation of liposomes (lipid vesicles) are used in liposome-protein binding assays, facilitated by avidin/streptavidin/NeutrAvidin and biotinylated phospholipid-containing liposomes. Here, we examined the effects of three spacers [six-carbon (X), polyethylene glycol (PEG) 180 (molecular weight 180) and PEG2000 (molecular weight 2,000)] between biotin and the phospholipid headgroup on the immobilization and sedimentation of small unilamellar liposomes/vesicles (SUVs). PEG180 and PEG2000 showed more efficient immobilization of biotinylated SUVs on NeutrAvidin-coated plates than X, but X and PEG180 showed more efficient sedimentation of biotinylated SUVs upon NeutrAvidin addition than PEG2000. Thus, the most appropriate spacers differed between immobilization and sedimentation. A spacer for biotinylated SUVs must be selected according to the particular liposome-protein binding assays examined.