A β-sheet-forming peptide conjugated with a water-soluble moiety (polyethylene glycol (PEG) or a transactivator of transcription (TAT) sequence) forms rod-like aggregates in aqueous solution. We explored the detailed structures of the aggregates using Synchrotron X-ray scattering. We found that the β-sheet-forming peptide indeed formed stacked β-sheets, in a manner similar to that observed in the case of amyloid protofilaments. We also found that the resultant rod-like objects could be completely dispersed in water, as a result of the hydrophilicity of PEG or TAT.
- Takuma Minami
- Sakiko Matsumoto
- Kazuo Sakurai
