β-Helical Fibrils from a Model Peptide

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 pre...

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Bibliographic Details
Published in:Biochemical and biophysical research communications 1997-06, Vol.235 (3), p.675-679
Main Authors: Lazo, N.D., Downing, Donald T.
Format: Article
Language:English
Subjects:
Amino Acid Sequence
Circular Dichroism
Magnetic Resonance Spectroscopy
Microscopy, Electron
Models, Molecular
Oligopeptides - chemical synthesis
Oligopeptides - chemistry
Protein Structure, Secondary
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Summary: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.
ISSN:0006-291X
1090-2104
DOI:10.1006/bbrc.1997.6863