Twisted Ribbon Aggregates in a Model Peptide System
(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
-
- 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}, }