Nanotubes and bilayers in a model peptide system
(2011) In Soft Matter 7(10). p.4868-4875- Abstract
- The trifluoroacetate (tfa) salt of the peptide (ala)(6)lys self-assembles in water into very long, hollow nanotubes with a radius R = 26 nm, above a critical aggregation concentration (volume fraction), phi(cac) = 0.10. The peptides carry a net positive charge that ensures colloidal stability of the self-assembly structures through a long-range electrostatic repulsion. There is only a weak temperature dependence of phi(cac) from which an enthalpy of aggregation of -k(B)T per molecule is estimated. SAXS data show that the thickness of the nanotube wall, delta, is less than 1 nm indicating that the peptides form a monolayer in the nanotube wall. The nanotubes have a very large aspect ratio and form an ordered nematic or hexagonal phase.... (More)
- The trifluoroacetate (tfa) salt of the peptide (ala)(6)lys self-assembles in water into very long, hollow nanotubes with a radius R = 26 nm, above a critical aggregation concentration (volume fraction), phi(cac) = 0.10. The peptides carry a net positive charge that ensures colloidal stability of the self-assembly structures through a long-range electrostatic repulsion. There is only a weak temperature dependence of phi(cac) from which an enthalpy of aggregation of -k(B)T per molecule is estimated. SAXS data show that the thickness of the nanotube wall, delta, is less than 1 nm indicating that the peptides form a monolayer in the nanotube wall. The nanotubes have a very large aspect ratio and form an ordered nematic or hexagonal phase. Because of the low delta/R ratio, the nanotube volume fraction grows very rapidly with increasing peptide concentration, phi, and reaches close packing already at phi = 0.15. When increasing the concentration further, there is a phase transition to a novel lamellar phase where the peptide molecules form bilayers consisting of two, presumably oppositely oriented, monolayers. (Less)
Please use this url to cite or link to this publication:
https://lup.lub.lu.se/record/1987081
- author
- Cenker, Celen LU ; Bucak, Seyda and Olsson, Ulf LU
- organization
- publishing date
- 2011
- type
- Contribution to journal
- publication status
- published
- subject
- in
- Soft Matter
- volume
- 7
- issue
- 10
- pages
- 4868 - 4875
- publisher
- Royal Society of Chemistry
- external identifiers
-
- wos:000290227400040
- scopus:79955652022
- ISSN
- 1744-6848
- DOI
- 10.1039/c0sm01186j
- language
- English
- LU publication?
- yes
- id
- 3b2719f7-6a60-4f9c-86a5-ae4e5bd50ab2 (old id 1987081)
- date added to LUP
- 2016-04-01 14:49:16
- date last changed
- 2022-01-28 02:42:21
@article{3b2719f7-6a60-4f9c-86a5-ae4e5bd50ab2,
abstract = {{The trifluoroacetate (tfa) salt of the peptide (ala)(6)lys self-assembles in water into very long, hollow nanotubes with a radius R = 26 nm, above a critical aggregation concentration (volume fraction), phi(cac) = 0.10. The peptides carry a net positive charge that ensures colloidal stability of the self-assembly structures through a long-range electrostatic repulsion. There is only a weak temperature dependence of phi(cac) from which an enthalpy of aggregation of -k(B)T per molecule is estimated. SAXS data show that the thickness of the nanotube wall, delta, is less than 1 nm indicating that the peptides form a monolayer in the nanotube wall. The nanotubes have a very large aspect ratio and form an ordered nematic or hexagonal phase. Because of the low delta/R ratio, the nanotube volume fraction grows very rapidly with increasing peptide concentration, phi, and reaches close packing already at phi = 0.15. When increasing the concentration further, there is a phase transition to a novel lamellar phase where the peptide molecules form bilayers consisting of two, presumably oppositely oriented, monolayers.}},
author = {{Cenker, Celen and Bucak, Seyda and Olsson, Ulf}},
issn = {{1744-6848}},
language = {{eng}},
number = {{10}},
pages = {{4868--4875}},
publisher = {{Royal Society of Chemistry}},
series = {{Soft Matter}},
title = {{Nanotubes and bilayers in a model peptide system}},
url = {{http://dx.doi.org/10.1039/c0sm01186j}},
doi = {{10.1039/c0sm01186j}},
volume = {{7}},
year = {{2011}},
}