Self-Assembly of a Designed Alternating Arginine/Phenylalanine Oligopeptide

A model octapeptide peptide consisting of an alternating sequence of arginine (Arg) and phenylalanine (Phe) residues, namely, [Arg-Phe]4, was prepared, and its self-assembly in solution studied. The simple alternating [Arg-Phe]4 peptide sequence allows for unique insights into the aggregation proces...

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Veröffentlicht in:Langmuir : the ACS journal of surfaces and colloids. - 1999. - 31(2015), 15 vom: 21. Apr., Seite 4513-23
1. Verfasser: Decandio, Carla C (VerfasserIn)
Weitere Verfasser: Silva, Emerson R, Hamley, Ian W, Castelletto, Valeria, Liberato, Michelle S, Oliveira, Vani X Jr, Oliveira, Cristiano L P, Alves, Wendel A
Format: Online-Aufsatz
Sprache:English
Veröffentlicht: 2015
Zugriff auf das übergeordnete Werk:Langmuir : the ACS journal of surfaces and colloids
Schlagworte:Journal Article Research Support, Non-U.S. Gov't Gels Oligopeptides Protein Aggregates Solutions Phenylalanine 47E5O17Y3R Arginine 94ZLA3W45F
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520 |a A model octapeptide peptide consisting of an alternating sequence of arginine (Arg) and phenylalanine (Phe) residues, namely, [Arg-Phe]4, was prepared, and its self-assembly in solution studied. The simple alternating [Arg-Phe]4 peptide sequence allows for unique insights into the aggregation process and the structure of the self-assembled motifs. Fluorescence and UV-vis assays were used to determine critical aggregation concentrations, corresponding to the formation of oligomeric species and β-sheet rich structures organized into both spheroidal aggregates and highly ordered fibrils. Electron and atomic force microscopy images show globular aggregates and long unbranched fibers with diameters ranging from ∼4 nm up to ∼40 nm. Infrared and circular dichroism spectroscopy show the formation of β-sheet structures. X-ray diffraction on oriented stalks show that the peptide fibers have an internal lamellar structure, with an orthorhombic unit cell with parameters a ∼ 27.6 Å, b ∼ 9.7 Å, and c ∼ 9.6 Å. In situ small-angle X-ray scattering (SAXS) shows the presence of low molecular weight oligomers in equilibrium with mature fibers which are likely made up from 5 or 6 intertwined protofilaments. Finally, weak gel solutions are probed under gentle shear, suggesting the ability of these arginine-rich fibers to form networks 
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650 7 |a Phenylalanine  |2 NLM 
650 7 |a 47E5O17Y3R  |2 NLM 
650 7 |a Arginine  |2 NLM 
650 7 |a 94ZLA3W45F  |2 NLM 
700 1 |a Silva, Emerson R  |e verfasserin  |4 aut 
700 1 |a Hamley, Ian W  |e verfasserin  |4 aut 
700 1 |a Castelletto, Valeria  |e verfasserin  |4 aut 
700 1 |a Liberato, Michelle S  |e verfasserin  |4 aut 
700 1 |a Oliveira, Vani X  |c Jr  |e verfasserin  |4 aut 
700 1 |a Oliveira, Cristiano L P  |e verfasserin  |4 aut 
700 1 |a Alves, Wendel A  |e verfasserin  |4 aut 
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