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Affinity partitioning of biotinylated mixed liposomes: effect of charge on biotin-NeutrAvidin interaction

Barinaga-Rementeria Ramírez, Irene LU ; Ekblad, Lars and Jergil, Bengt LU (2000) In Journal of Chromatography. B, Biomedical Sciences and Applications 743(1-2). p.389-396
Abstract
The partitioning behaviour of biotinylated mixed liposomes in aqueous poly(ethylene glycol)/dextran two-phase systems containing NeutrAvidin-dextran suggests that the biotin-NeutrAvidin affinity interaction is charge dependent. Biotinylated phosphatidylcholine liposomes with a low negative surface charge distributed in the NeutrAvidin-containing bottom phase at neutral pH, but the introduction of additional negative charges by including phosphatidylserine or the surfactant sodium dodecylsulfate in the liposomes caused them to distribute in the poly(ethylene glycol)-rich top phase instead. By gradually lowering the pH of the affinity two-phase system below the isoelectric point (6.3) of NeutrAvidin, negatively charged... (More)
The partitioning behaviour of biotinylated mixed liposomes in aqueous poly(ethylene glycol)/dextran two-phase systems containing NeutrAvidin-dextran suggests that the biotin-NeutrAvidin affinity interaction is charge dependent. Biotinylated phosphatidylcholine liposomes with a low negative surface charge distributed in the NeutrAvidin-containing bottom phase at neutral pH, but the introduction of additional negative charges by including phosphatidylserine or the surfactant sodium dodecylsulfate in the liposomes caused them to distribute in the poly(ethylene glycol)-rich top phase instead. By gradually lowering the pH of the affinity two-phase system below the isoelectric point (6.3) of NeutrAvidin, negatively charged phosphatidylserine/phosphatidylcholine liposomes increasingly were attracted by NeutrAvidin to the bottom phase. It is suggested that acidic amino acids present at the rim of the biotin-binding pocket of NeutrAvidin may interact electrostatically with charged residues of the closely apposed liposome surface affecting the affinity interaction. (Less)
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author
organization
publishing date
type
Contribution to journal
publication status
published
subject
keywords
Phospholipids, NeutrAvidin, Biotin
in
Journal of Chromatography. B, Biomedical Sciences and Applications
volume
743
issue
1-2
pages
389 - 396
publisher
Elsevier
external identifiers
  • scopus:0343517652
ISSN
1387-2273
DOI
10.1016/S0378-4347(00)00065-7
language
English
LU publication?
yes
id
ae60377a-8fa9-4a4d-87fa-fa4cd73ed13f (old id 125076)
date added to LUP
2007-07-04 11:07:31
date last changed
2017-01-01 07:27:20
@article{ae60377a-8fa9-4a4d-87fa-fa4cd73ed13f,
  abstract     = {The partitioning behaviour of biotinylated mixed liposomes in aqueous poly(ethylene glycol)/dextran two-phase systems containing NeutrAvidin-dextran suggests that the biotin-NeutrAvidin affinity interaction is charge dependent. Biotinylated phosphatidylcholine liposomes with a low negative surface charge distributed in the NeutrAvidin-containing bottom phase at neutral pH, but the introduction of additional negative charges by including phosphatidylserine or the surfactant sodium dodecylsulfate in the liposomes caused them to distribute in the poly(ethylene glycol)-rich top phase instead. By gradually lowering the pH of the affinity two-phase system below the isoelectric point (6.3) of NeutrAvidin, negatively charged phosphatidylserine/phosphatidylcholine liposomes increasingly were attracted by NeutrAvidin to the bottom phase. It is suggested that acidic amino acids present at the rim of the biotin-binding pocket of NeutrAvidin may interact electrostatically with charged residues of the closely apposed liposome surface affecting the affinity interaction.},
  author       = {Barinaga-Rementeria Ramírez, Irene and Ekblad, Lars and Jergil, Bengt},
  issn         = {1387-2273},
  keyword      = {Phospholipids,NeutrAvidin,Biotin},
  language     = {eng},
  number       = {1-2},
  pages        = {389--396},
  publisher    = {Elsevier},
  series       = {Journal of Chromatography. B, Biomedical Sciences and Applications},
  title        = {Affinity partitioning of biotinylated mixed liposomes: effect of charge on biotin-NeutrAvidin interaction},
  url          = {http://dx.doi.org/10.1016/S0378-4347(00)00065-7},
  volume       = {743},
  year         = {2000},
}