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Aqueous Self-Assembly within the Homologous Peptide Series A(n)K

Cenker, Celen LU ; Bucak, Seyda and Olsson, Ulf LU (2014) In Langmuir 30(33). p.10072-10079
Abstract
We compare the aqueous self-assembly behavior within the homologous peptide series A(n)K, where A is alanine, K is lysine, and n = 4, 6, 8, and 10. The aqueous peptide solubility, phi(s) (volume fraction), depends strongly on the number of hydrophobic alanine residues and decreases approximately as phi(s) approximate to 10(-n). Also the self-assembly structure depends on n. A(4)K is highly water-soluble and shows no relevant self-assembly. A(6)K, which has been extensively studied previously, forms hollow nanotubes in water. A(8)K and A(10)K self-assembly is characterized here using a combination of small- and wide-angle X-ray scattering, static and dynamic light scattering, cryo transmission electron microscopy, and circular dichroism... (More)
We compare the aqueous self-assembly behavior within the homologous peptide series A(n)K, where A is alanine, K is lysine, and n = 4, 6, 8, and 10. The aqueous peptide solubility, phi(s) (volume fraction), depends strongly on the number of hydrophobic alanine residues and decreases approximately as phi(s) approximate to 10(-n). Also the self-assembly structure depends on n. A(4)K is highly water-soluble and shows no relevant self-assembly. A(6)K, which has been extensively studied previously, forms hollow nanotubes in water. A(8)K and A(10)K self-assembly is characterized here using a combination of small- and wide-angle X-ray scattering, static and dynamic light scattering, cryo transmission electron microscopy, and circular dichroism spectroscopy. They both form similar thin rodlike aggregates with lengths on the order of 100 nm and a biaxial cross-section with dimensions of 4 nrn x 8 nm. We show that different sample preparation protocols result in different lengths of the A(10)K rodlike aggregates. On the basis of these findings, the question of thermodynamic equilibrium of peptide self-assembly is discussed. (Less)
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author
organization
publishing date
type
Contribution to journal
publication status
published
subject
in
Langmuir
volume
30
issue
33
pages
10072 - 10079
publisher
The American Chemical Society
external identifiers
  • wos:000340993200025
  • scopus:84906689606
ISSN
0743-7463
DOI
10.1021/la5016324
language
English
LU publication?
yes
id
95a6547c-4631-46b1-ae94-a186eb4cca0c (old id 4648968)
date added to LUP
2014-09-24 09:13:39
date last changed
2017-01-01 03:20:32
@article{95a6547c-4631-46b1-ae94-a186eb4cca0c,
  abstract     = {We compare the aqueous self-assembly behavior within the homologous peptide series A(n)K, where A is alanine, K is lysine, and n = 4, 6, 8, and 10. The aqueous peptide solubility, phi(s) (volume fraction), depends strongly on the number of hydrophobic alanine residues and decreases approximately as phi(s) approximate to 10(-n). Also the self-assembly structure depends on n. A(4)K is highly water-soluble and shows no relevant self-assembly. A(6)K, which has been extensively studied previously, forms hollow nanotubes in water. A(8)K and A(10)K self-assembly is characterized here using a combination of small- and wide-angle X-ray scattering, static and dynamic light scattering, cryo transmission electron microscopy, and circular dichroism spectroscopy. They both form similar thin rodlike aggregates with lengths on the order of 100 nm and a biaxial cross-section with dimensions of 4 nrn x 8 nm. We show that different sample preparation protocols result in different lengths of the A(10)K rodlike aggregates. On the basis of these findings, the question of thermodynamic equilibrium of peptide self-assembly is discussed.},
  author       = {Cenker, Celen and Bucak, Seyda and Olsson, Ulf},
  issn         = {0743-7463},
  language     = {eng},
  number       = {33},
  pages        = {10072--10079},
  publisher    = {The American Chemical Society},
  series       = {Langmuir},
  title        = {Aqueous Self-Assembly within the Homologous Peptide Series A(n)K},
  url          = {http://dx.doi.org/10.1021/la5016324},
  volume       = {30},
  year         = {2014},
}