Twisted Ribbon Aggregates in a Model Peptide System
Rüter, Axel LU
; Kuczera, Stefan
LU
; Pochan, Darrin J.
and Olsson, Ulf
LU
(2019)
In Langmuir
35(17).
p.5802-5808
- Abstract
The model peptides A 8 K and A 10 K self-assemble in water into ca. 100 nm long ribbon-like aggregates. These structures can be described as β-sheets laminated into a ribbon structure with a constant elliptical cross-section of 4 by 8 nm, where the longer axis corresponds to a finite number, N ≠15, of laminated sheets, and 4 nm corresponds to a stretched peptide length. The ribbon cross-section is strikingly constant and independent of... (More)
The model peptides A 8 K and A 10 K self-assemble in water into ca. 100 nm long ribbon-like aggregates. These structures can be described as β-sheets laminated into a ribbon structure with a constant elliptical cross-section of 4 by 8 nm, where the longer axis corresponds to a finite number, N ≠15, of laminated sheets, and 4 nm corresponds to a stretched peptide length. The ribbon cross-section is strikingly constant and independent of the peptide concentration. High-contrast transmission electron microscopy shows that the ribbons are twisted with a pitch λ ≠15 nm. The self-assembly is analyzed within a simple model taking into account the interfacial free energy of the hydrophobic β-sheets and a free energy penalty arising from an increased stretching of hydrogen bonds within the laminated β-sheets, arising from the twist of the ribbons. The model predicts an optimal value N, in agreement with the experimental observations.
(Less)
- author
- Rüter, Axel
LU
; Kuczera, Stefan
LU
; Pochan, Darrin J.
and Olsson, Ulf
LU
- organization
- publishing date
- 2019
- type
- Contribution to journal
- publication status
- published
- subject
- in
- Langmuir
- volume
- 35
- issue
- 17
- pages
- 7 pages
- publisher
- The American Chemical Society (ACS)
- external identifiers
-
- scopus:85065148632
- pmid:30955339
- ISSN
- 0743-7463
- DOI
- 10.1021/acs.langmuir.8b03886
- language
- English
- LU publication?
- yes
- id
- fa4cdbde-09e3-44f8-8ed2-e2cce467b805
- date added to LUP
- 2019-05-15 14:29:47
- date last changed
- 2024-04-02 04:09:14
@article{fa4cdbde-09e3-44f8-8ed2-e2cce467b805,
abstract = {{<p> The model peptides A <sub>8</sub> K and A <sub>10</sub> K self-assemble in water into ca. 100 nm long ribbon-like aggregates. These structures can be described as β-sheets laminated into a ribbon structure with a constant elliptical cross-section of 4 by 8 nm, where the longer axis corresponds to a finite number, N ≠15, of laminated sheets, and 4 nm corresponds to a stretched peptide length. The ribbon cross-section is strikingly constant and independent of the peptide concentration. High-contrast transmission electron microscopy shows that the ribbons are twisted with a pitch λ ≠15 nm. The self-assembly is analyzed within a simple model taking into account the interfacial free energy of the hydrophobic β-sheets and a free energy penalty arising from an increased stretching of hydrogen bonds within the laminated β-sheets, arising from the twist of the ribbons. The model predicts an optimal value N, in agreement with the experimental observations.</p>}},
author = {{Rüter, Axel and Kuczera, Stefan and Pochan, Darrin J. and Olsson, Ulf}},
issn = {{0743-7463}},
language = {{eng}},
number = {{17}},
pages = {{5802--5808}},
publisher = {{The American Chemical Society (ACS)}},
series = {{Langmuir}},
title = {{Twisted Ribbon Aggregates in a Model Peptide System}},
url = {{http://dx.doi.org/10.1021/acs.langmuir.8b03886}},
doi = {{10.1021/acs.langmuir.8b03886}},
volume = {{35}},
year = {{2019}},
}