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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.

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author
; ; and
organization
publishing date
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
  • pmid:30955339
  • scopus:85065148632
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
2021-04-13 05:45:18
@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},
}