Organization of designed nanofibrils assembled from alpha-helical peptides as determined by electron microscopy.
Self-assembling peptides present attractive platforms for engineering materials with controlled nanostructures. Recently, an alpha-helical fibril forming peptide (alphaFFP) was designed that self-assembles into nanofibrils at acid pH. Circular dichroism spectroscopy, electron-microscopy and x-ray fibre diffraction data showed that the most likely structure of alphaFFP fibrils is a five-stranded coiled coil rope. In the present study, scanning transmission electron microscopy (STEM) was used to improve our understanding of the alphaFFP fibril structure. The measurements of fibril mass per length suggest that there are ten alpha-helices in transverse sections of the fibrils. Based on the known data, it is proposed that a predominant fibrillar structure of alphaFFP is a dimer of alpha-helical five stranded protofilaments wrapped around a common axis. It is shown that these structures have an axial dimension of 58 +/- 16 nm and a width of 4 +/- 1 nm. A small number of thin fibrils is also observed in the negative stained preparation and STEM images. The thin fibrils may correspond to the single protofilament.
Kajava
Andrey V
AV
Center for Molecular Modeling, CIT, National Institutes of Health, Bethesda, MD 20892, USA. kajava@cnrs-mop.fr
Potekhin
Sergey A
SA
Corradin
Giampietro
G
Leapman
Richard D
RD
D008855:Microscopy, Electron, Scanning; D008958:Models, Molecular; D010446:Peptide Fragments / Q000737:chemistry* / Q000648:ultrastructure*; D017433:Protein Structure, Secondary; D013329:Structure-Activity Relationship
D010446:Peptide Fragments