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Peptide nanospheres self‐assembled from a modified β‐annulus peptide of Sesbania mosaic virus

A novel β‐annulus peptide of Sesbania mosaic virus bearing an FKFE sequence at the C terminus was synthesized, and its self‐assembling behavior in water was investigated. Dynamic light scattering and transmission electron microscopy showed that the β‐annulus peptide bearing an FKFE sequence self‐assembled into approximately 30 nm nanospheres in water at pH 3.8, whereas the β‐annulus peptide without the FKFE sequence afforded only irregular aggregates. The peptide nanospheres possessed a definite critical aggregation concentration (CAC = 26 μM), above which the size of nanospheres were nearly unaffected by the peptide concentration. The formation of peptide nanospheres was significantly affected by pH; the peptide did not form any assemblies at pH 2.2, whereas larger aggregates were formed at pH 6.4–11.6. © 2015 Wiley Periodicals, Inc. Biopolymers (Pept Sci) 106: 470–475, 2016.