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Updated: Jun 8, 2026

Formation of Ordered Biomolecular Structures by the Self-assembly of Short Peptides
Published on: November 21, 2013
PbSe nanocrystal growth as nanocubes and nanorods on peptide nanotubes via different directed-assembly pathways
Menglu Shi1, Wei Su, Hiroshi Matsui
1Department of Chemistry and Biochemistry, City University of New York - Hunter College, New York, NY 10065, USA.
Abstract:
Pb-binding TAR-1 peptides (Ile-Ser-Leu-Leu-His-Ser-Thr) were covalently conjugated on a bolaamphiphile peptide nanotube substrate and the precursors of PbSe were incubated at room temperature. This resulted in the growth of highly crystalline PbSe nanocubes on this biomimetic cylindrical substrate. The growth mechanism to generate nanocubes occurs via the directed self-assembly of nanoparticles and then nanoparticle fusion. The peptide conformation and the cylindrical peptide nanotube substrate play important roles in the mesoscopic crystallization of PbSe nanocubes. Changing the buffer for the peptide immobilization process from 2-(N-morpholino)ethanesulfonic acid to phosphate induces a transformation in the nanocrystal shape from nanocube to nanorods. The conformational change of the TAR-1 peptide on the nanotubes due to the change in the buffer seems to be responsible for aggregating intermediate nanoparticles in different directions for the directed fusion and mesoscopic crystallization of PbSe into the different shapes.

