for peptides. How peptides interact with the SDS micelle Binding affinities of tryptophan dipeptides, Trp-X (X Γ A, F, G, and how their structures change in the media have been I, K, L, S, T, V, W, and Y), X-Trp (X Γ A, F, G, K, L, P, R, V, discussed (5-7). Results indicating that some of the rela-W
Interaction of main-chain polycations with sodium dodecyl sulfate
β Scribed by Xiaoliang Zheng; Weixiao Cao
- Publisher
- John Wiley and Sons
- Year
- 2001
- Tongue
- English
- Weight
- 104 KB
- Volume
- 50
- Category
- Article
- ISSN
- 0959-8103
- DOI
- 10.1002/pi.645
No coin nor oath required. For personal study only.
β¦ Synopsis
Abstract
The interaction of the mainβchain polycations 2,2βionene (I~2,2~) and 3,3βionene (I~3,3~) with sodium dodecyl sulfate (SDS) has been investigated in aqueous solution. It was confirmed that the interaction is cooperative and a stoichiometric 1:1 complex of I~2,2~βSDS or I~3,3~βSDS with regular structure forms as a precipitate irrespective of the molar ratio of the components. It is completely different from the interaction of sideβchain polycations such as the poly[(vinyl pyridine)βcoβstyrene] copolymer cation (PVSC) with SDS, in which no cooperative effect was observed. The driving force responsible for the cooperative effect is believed to be the hydrophobic attraction between the SDS molecule already linked on the ionene chain and the next SDS molecule to be entered. It was also confirmed that the structures of the complexes are very different, ie the ioneneβSDS complexes exhibit high regularity whereas the PVSCβSDS complex is irregular.
Β© 2001 Society of Chemical Industry
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