Self-Assembly of Peptide Nanotubes in an Organic Solvent

Citations Over TimeTop 10% of 2008 papers

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.

Related Papers

• → Molecular basis of film formation from a soybean protein: comparison between the conformation of glycinin in aqueous solution and in films(1998)145 cited
• → Protein Denaturation with Guanidinium: A 2D-IR Study(2013)62 cited
• → Predicting protein secondary structure using continuous wavelet transform and Chou-Fasman method(2005)11 cited
• → Composite Nanotube Ring Structures Formed by Two-Step Self-Assembly for Drug Loading/Release(2019)9 cited
• → The predicted secondary structure of enolase(1986)17 cited