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Protein Science, Vol 7, Issue 7 1545-1554, Copyright © 1998 by Cold Spring Harbor Laboratory Press

ARTICLE

Engineering of betabellin-15D: A 64 residue beta sheet protein that forms long narrow multimeric fibrils

A. LIM, M. J. SADERHOLM, A. M. MAKHOV, M. KROLL, Y. YAN, L. PERERA, J. D. GRIFFITH and B. W. ERICKSON
Department of Chemistry, The University of North Carolina at Chapel Hill, Chapel Hill, North Carolina 27599

The betabellin target structure is a {beta}-sandwich protein consisting of two 32 residue {beta}-sheets packed against one another by interaction of their hydrophobic faces. The 32 residue chain of betabellin-15S (HSLTAKIpkLTFSIAphTYTCAV pkYTAKVSH, where p = DPro, k = DLys, and h = DHis) did not fold in water at pH 6.5. Air oxidation of betabellin-15S provided betabellin-15D, the 64 residue disulfide bridged two-chain molecule, which also remained unfolded in water at pH 6.5. By circular dichroic spectropolarimetry, the extent of {beta} structure observed for betabellin-15D increased with the pH and ionic strength of the solution and the betabellin-15D concentration. By electron microscopy, in 5.0 mM MOPS and 0.25 M NaCl at pH 6.9, betabellin-15D formed long narrow multimeric fibrils. A molecular model was constructed to show that the dimensions of these betabellin-15D fibrils are consistent with a single row of {beta}-sandwich molecules joined by multiple intersheet H-bonds.
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