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Partitioning of hydrophobic amino acids and oligopeptides in aqueous two-phase system containing self-aggregating block copolymer - Effects of temperature, salts and surfactants

Svensson, Mårten; Joabsson, Fredrik; Linse, Per LU and Tjerneld, Folke LU (1997) In Journal of Chromatography A 761(1-2). p.91-101
Abstract
The partitioning of hydrophobic amino acids and oligopeptides in the Pluronic P105-dextran-water system has been studied. Pluronic P105 is a member of a family of triblock copolymers with the structure PEO-PPO-PEO, where PEO is poly(ethylene oxide) and PPO poly(propylene oxide). The partitioning was studied for tryptophan, phenylalanine and di- and tri-peptides composed of these amino acids at 5 and 40oC. These temperatures correspond to a unimeric (5oC) and a micellar (40oC) state of the P105 molecule. Partitioning depended strongly on the temperature which is attributed to the increased hydrophobicity of Pluronic P105 with increasing temperature. However, it appears that the presence of the micelles plays no major direct role. The effect... (More)
The partitioning of hydrophobic amino acids and oligopeptides in the Pluronic P105-dextran-water system has been studied. Pluronic P105 is a member of a family of triblock copolymers with the structure PEO-PPO-PEO, where PEO is poly(ethylene oxide) and PPO poly(propylene oxide). The partitioning was studied for tryptophan, phenylalanine and di- and tri-peptides composed of these amino acids at 5 and 40oC. These temperatures correspond to a unimeric (5oC) and a micellar (40oC) state of the P105 molecule. Partitioning depended strongly on the temperature which is attributed to the increased hydrophobicity of Pluronic P105 with increasing temperature. However, it appears that the presence of the micelles plays no major direct role. The effect of different pH, salts and surfactants (both cationic and anionic) on partitioning has also been investigated. (Less)
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author
organization
publishing date
type
Contribution to journal
publication status
published
subject
keywords
Partitioning, Temperature effects, Amino acids, Peptides, Pluronic P105, Tryptophan, Phenylalanine
in
Journal of Chromatography A
volume
761
issue
1-2
pages
91 - 101
publisher
Elsevier
external identifiers
  • scopus:0031566997
ISSN
0021-9673
DOI
10.1016/S0021-9673(96)00830-8
language
English
LU publication?
yes
id
fa5a538f-3583-4326-8858-d3b507338503 (old id 126238)
date added to LUP
2007-07-06 16:41:44
date last changed
2017-01-01 07:28:09
@article{fa5a538f-3583-4326-8858-d3b507338503,
  abstract     = {The partitioning of hydrophobic amino acids and oligopeptides in the Pluronic P105-dextran-water system has been studied. Pluronic P105 is a member of a family of triblock copolymers with the structure PEO-PPO-PEO, where PEO is poly(ethylene oxide) and PPO poly(propylene oxide). The partitioning was studied for tryptophan, phenylalanine and di- and tri-peptides composed of these amino acids at 5 and 40oC. These temperatures correspond to a unimeric (5oC) and a micellar (40oC) state of the P105 molecule. Partitioning depended strongly on the temperature which is attributed to the increased hydrophobicity of Pluronic P105 with increasing temperature. However, it appears that the presence of the micelles plays no major direct role. The effect of different pH, salts and surfactants (both cationic and anionic) on partitioning has also been investigated.},
  author       = {Svensson, Mårten and Joabsson, Fredrik and Linse, Per and Tjerneld, Folke},
  issn         = {0021-9673},
  keyword      = {Partitioning,Temperature effects,Amino acids,Peptides,Pluronic P105,Tryptophan,Phenylalanine},
  language     = {eng},
  number       = {1-2},
  pages        = {91--101},
  publisher    = {Elsevier},
  series       = {Journal of Chromatography A},
  title        = {Partitioning of hydrophobic amino acids and oligopeptides in aqueous two-phase system containing self-aggregating block copolymer - Effects of temperature, salts and surfactants},
  url          = {http://dx.doi.org/10.1016/S0021-9673(96)00830-8},
  volume       = {761},
  year         = {1997},
}