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- W2012093336 abstract "A tripeptide containing an Aib (α-amino isobutyric acid) residue self-assembles to form porous nanomaterials in solid state. In spite of having a hollow nanotubular structure, the self-assembly nature of the peptide is different, which leads to the formation of pores with different internal diameters. The single-crystal X-ray diffraction study reveals that the peptide forms continuous hydrogen-bonded poly-disperse nanopores (3, 5 and 8 membered) starting from the β-turn conformation as an associating sub-unit. The field emission scanning electron micrograph (FESEM) shows that the average pore sizes are in the range of 20 to 200 nm, although a few large pores are also visible. Moreover, the peptide 1 acts as an in situ reducing agent to synthesize hexagonal gold nanoparticles (GNP)." @default.
- W2012093336 created "2016-06-24" @default.
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- W2012093336 date "2011-01-01" @default.
- W2012093336 modified "2023-10-14" @default.
- W2012093336 title "Insights into self-assembling nanoporous peptide and in situ reducing agent" @default.
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- W2012093336 doi "https://doi.org/10.1039/c0ce00143k" @default.
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