Amyloid-like Fibrils from a Diphenylalanine Capped with an Aromatic Fluorenyl
The self-assembly behavior of a diphenylalanine amphiphile blocked at the C-terminus with a 9-fluorenylmethyl ester and stabilized at the N-terminus with a trifluoroacetate (TFA) anion, TFA·FF-OFm, has been examined. At low peptide concentration (0.5 mg/mL), long amyloid-like fibrils, which come fro...
| Publié dans: | Langmuir : the ACS journal of surfaces and colloids. - 1985. - 34(2018), 50 vom: 18. Dez., Seite 15551-15559 |
|---|---|
| Auteur principal: | |
| Autres auteurs: | , , , , , , , , |
| Format: | Article en ligne |
| Langue: | English |
| Publié: |
2018
|
| Accès à la collection: | Langmuir : the ACS journal of surfaces and colloids |
| Sujets: | Journal Article Research Support, Non-U.S. Gov't Dipeptides Fluorenes Peptides phenylalanylphenylalanine 2577-40-4 Phenylalanine 47E5O17Y3R |
| Résumé: | The self-assembly behavior of a diphenylalanine amphiphile blocked at the C-terminus with a 9-fluorenylmethyl ester and stabilized at the N-terminus with a trifluoroacetate (TFA) anion, TFA·FF-OFm, has been examined. At low peptide concentration (0.5 mg/mL), long amyloid-like fibrils, which come from the fusion of two or more helical ribbons and/or thinner fibrils, organized in bundles or as individual entities are detected. Microbeam synchrotron radiation infrared spectroscopy has shown that TFA·FF-OFm molecules in amyloid-like fibrils arrange, forming antiparallel β-sheets. Alteration of the experimental conditions to prioritize the thermodynamic contribution with respect to the kinetic one in the self-assembly process inhibits the organization of amyloid-like structures in favor of the formation of conventional fibrous structures. On the basis of experimental observations, a structural model where the individual antiparallel β-sheets are oriented in parallel has been proposed for TFA·FF-OFm amyloid-like fibrils |
|---|---|
| Description: | Date Completed 03.04.2019 Date Revised 04.12.2021 published: Print-Electronic Citation Status MEDLINE |
| ISSN: | 1520-5827 |
| DOI: | 10.1021/acs.langmuir.8b03378 |