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...

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Veröffentlicht in:Langmuir : the ACS journal of surfaces and colloids. - 1999. - 34(2018), 50 vom: 18. Dez., Seite 15551-15559
1. Verfasser: Martí, Didac (VerfasserIn)
Weitere Verfasser: Mayans, Enric, Gil, Ana M, Díaz, Angélica, Jiménez, Ana I, Yousef, Ibraheem, Keridou, Ina, Cativiela, Carlos, Puiggalí, Jordi, Alemán, Carlos
Format: Online-Aufsatz
Sprache:English
Veröffentlicht: 2018
Zugriff auf das übergeordnete Werk:Langmuir : the ACS journal of surfaces and colloids
Schlagworte:Journal Article Research Support, Non-U.S. Gov't Dipeptides Fluorenes Peptides phenylalanylphenylalanine 2577-40-4 Phenylalanine 47E5O17Y3R
Beschreibung
Zusammenfassung: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
Beschreibung: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