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EnglishWithin the homologous series of amphiphilic peptides AnK, both A8K and A10K self-assemble in water to form twisted ribbon fibrils with lengths around 100 nm. The structure of the fibrils can be described in terms of twisted β-sheets extending in the direction of the fibrils, laminated to give a constant cross section of 4 nm by 8 nm. The finite width of the twisted ribbons can be reasonably explained within a simple thermodynamic model, considering a free energy penalty for the stretching of hydrogen bonds along the twisted β-sheets and an interfacial free energy gain for the lamination of the hydrophobic β-sheets. In this study, we characterize the self-assembly behavior of these peptides in nonaqueous solutions as a route to probe the role of hydrophobic interaction in fibril stabilization. Both peptides, in methanol and N,N-dimethylformamide, were found to form fibrillar aggregates with the same β-sheet structure as in water but with slightly smaller cross-sectional sizes. However, the gel-like texture, the slow relaxation in dynamic light scattering experiments, and a correlation peak in the small-angle X-ray scattering pattern highlighted enhanced interfibril interactions in the nonaqueous solvents in the same concentration range. This could be ascribed to a higher effective volume of the aggregates because of enhanced fibril growth and length, as suggested by light scattering and cryogenic transmission electron microscopy analyses. These effects can be discussed considering how the solvent properties affect the different energetic contributions (hydrophobic, electrostatic, and hydrogen bonding) to fibril formation. In the analyzed case, the decreased hydrogen bonding propensity of the nonaqueous solvents makes the hydrogen bond formation along the fibril a key driving force for peptide assembly, whereas it represents a nonrelevant contribution in water. Copyright © 2020 American Chemical Society.
Self-Assembly of model amphiphilic peptides in nonaqueous solvents: changing the driving force for aggregation does not change the fibril structure / Del Giudice, Alessandra; Rüter, Axel; Pavel, Nicolae Viorel; Galantini, Luciano; Olsson, Ulf. - In: LANGMUIR. - ISSN 0743-7463. - 36:29(2020), pp. 8451-8460. [10.1021/acs.langmuir.0c00876]
| Titolo: | Self-Assembly of model amphiphilic peptides in nonaqueous solvents: changing the driving force for aggregation does not change the fibril structure | |
| Autori: | ||
| Data di pubblicazione: | 2020 | |
| Rivista: | ||
| Citazione: | Self-Assembly of model amphiphilic peptides in nonaqueous solvents: changing the driving force for aggregation does not change the fibril structure / Del Giudice, Alessandra; Rüter, Axel; Pavel, Nicolae Viorel; Galantini, Luciano; Olsson, Ulf. - In: LANGMUIR. - ISSN 0743-7463. - 36:29(2020), pp. 8451-8460. [10.1021/acs.langmuir.0c00876] | |
| Handle: | http://hdl.handle.net/11573/1463306 | |
| Appartiene alla tipologia: | 01a Articolo in rivista |
File allegati a questo prodotto
| File | Note | Tipologia | Licenza | |
|---|---|---|---|---|
| DelGiudice_Self-Assembly_2020_PrePrint.pdf | https://doi.org/10.1021/acs.langmuir.0c00876 | Documento in Pre-print (manoscritto inviato all'editore, precedente alla peer review) |  | Open Access Visualizza/Apri |
| DelGiudice_Self-Assembly_2020.pdf | https://doi.org/10.1021/acs.langmuir.0c00876 | Versione editoriale (versione pubblicata con il layout dell'editore) |  | Open Access Visualizza/Apri |
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