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Biophys J, September 2002, p. 1716-1727, Vol. 83, No. 3

Molecular Organization of Amyloid Protofilament-Like Assembly of Betabellin 15D: Helical Array of beta -Sandwiches

Hideyo Inouye,* Jeremy E. Bond,* Sean P. Deverin,* Amareth Lim,dagger Catherine E. Costello,dagger and Daniel A. Kirschner*

 *Biology Department, Boston College, Chestnut Hill, Massachusetts 02467-3811 and  dagger Department of Biochemistry, Boston University School of Medicine, Boston, Massachusetts 02118-2526 USA

Betabellin is a 32-residue peptide engineered to fold into a four-stranded antiparallel beta -sheet protein. Upon air oxidation, the betabellin peptides can fold and assemble into a disulfide-bridged homodimer, or beta -sandwich, of 64 residues. Recent biophysical and ultrastructural studies indicate that betabellin 15D (B15D) (a homodimer of HSLTAKIpkLTFSIAphTYTCAVpkYTAKVSH, where p = DPro, k = DLys, and h = DHis) forms unbranched, 35-Å wide assemblies that resemble the protofilaments of amyloid fibers. In the present study, we have analyzed in detail the X-ray diffraction patterns of B15D prepared from acetonitrile. The fiber diffraction analysis indicated that the B15D fibril was composed of a double helix defined by the selection rule l = n + 7m (where l is even, and n and m are any integers), and having a 199-Å period and pitch, 28-Å rise per unit, and 10-Å radius. This helical model is equivalent to a reverse-handed, single helix with half the period and defined by the selection rule l = -3n + 7m (where l is any integer). The asymmetric unit is the single B15D beta -sandwich molecule. These results suggest that the betabellin assembly that models the protofilaments of amyloid fibers is made up of discrete subunits on a helical array. Multiple intersheet hydrogen bonds in the axial direction and intersandwich polar interactions in the lateral direction stabilize the array.

Biophys J, September 2002, p. 1716-1727, Vol. 83, No. 3
© 2002 by the Biophysical Society   0006-3495/02/09/1716/12  $2.00


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