Partitioning of hydrophobic amino acids and oligopeptides in aqueous two-phase system containing self-aggregating block copolymer - Effects of temperature, salts and surfactants
(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)
Please use this url to cite or link to this publication:
https://lup.lub.lu.se/record/126238
- author
- Svensson, Mårten ; Joabsson, Fredrik ; Linse, Per LU and Tjerneld, Folke LU
- organization
- publishing date
- 1997
- 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
- 2016-04-01 17:14:24
- date last changed
- 2022-01-29 01:17:15
@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}}, keywords = {{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}}, doi = {{10.1016/S0021-9673(96)00830-8}}, volume = {{761}}, year = {{1997}}, }