title: Peptide nanospheres self-assembled from a modified β-annulus peptide of Sesbania mosaic virus.
abstract: 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.
authors.affiliation: Department of Chemistry and Biotechnology, Graduate School of Engineering, Tottori University, Tottori, Japan.
authors.forename: Kazunori
authors.initials: K
authors.lastname: Matsuura
authors.affiliation: Department of Chemistry and Biochemistry, Graduate School of Engineering, Kyushu University, Fukuoka, Japan.
authors.forename: Yusaku
authors.initials: Y
authors.lastname: Mizuguchi
authors.affiliation: Department of Chemistry and Biochemistry, Graduate School of Engineering, Kyushu University, Fukuoka, Japan.
authors.forename: Nobuo
authors.initials: N
authors.lastname: Kimizuka
mesh_terms: D009029:Mosaic Viruses / Q000737:chemistry*; D054118:Nanospheres / Q000737:chemistry*; D010455:Peptides / Q000138:chemical synthesis / Q000737:chemistry; D049931:Sesbania / Q000821:virology*; D014764:Viral Proteins / Q000737:chemistry*
chemical_list: D010455:Peptides; D014764:Viral Proteins
keywords: nanosphere; self-assembly; viral capsid; β-annulus peptide