Abstract
A synthetic peptide, KLEG13 (Ac-KLKLKLELELELG-NH2), composed of alternating bulky hydrophilic and hydrophobic amino acid residues formed clear, viscous dispersions of fibrils in saline solutions. The fibrils had a uniform diameter of 2 nm as measured on electron micrographs of negatively stained preparations.13C solid-state nuclear magnetic resonance spectroscopy of the fibrils indicated the presence of a β-conformation. Circular dichroic spectra of the dispersion of fibrils were essentially identical to the calculated spectrum of a 100% β-helix. Space-filling CPK models of a proposed β-helical conformation of the peptide, in which the leucine side chains form a hydrophobic core and the hydrophilic lysine and glutamate side chains extend outwards from the helix, had a diameter consistent with the observed 2-nm diameter of the fibrils. This study may have implications regarding the structure of amyloid fibrils.
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