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Title: Self-assembly of Peptide nanotubes in an organic solvent. Author: Krysmann MJ, Castelletto V, McKendrick JE, Clifton LA, W Hamley I, Harris PJ, King SM. Journal: Langmuir; 2008 Aug 05; 24(15):8158-62. PubMed ID: 18572891. Abstract: The self-assembly of a modified fragment of the amyloid beta peptide, based on sequence Abeta(16-20), KLVFF, extended to give AAKLVFF is studied in methanol. Self-assembly into peptide nanotubes is observed, as confirmed by electron microscopy and small-angle X-ray scattering. The secondary structure of the peptide is probed by FTIR and circular dichroism, and UV/visible spectroscopy provides evidence for the important role of aromatic interactions between phenylalanine residues in driving beta-sheet self-assembly. The beta-sheets wrap helically to form the nanotubes, the nanotube wall comprising four wrapped beta-sheets. At higher concentration, the peptide nanotubes form a nematic phase that exhibits spontaneous flow alignment as observed by small-angle neutron scattering.[Abstract] [Full Text] [Related] [New Search]