Large amyloid fibers of predictable morphology and properties can be self-assembled through a known hierarchy of scale. The key to achieving large-scale structures is to use a two protein mixture where one protein is a hydrophobic �template� protein and the other a predominantly hydrophilic, a-helical �adder� protein. The two proteins work cooperatively to build across scales. Part of the cooperative mechanism involves a to � conformation change of the adder protein to build into the structure. Here, adder proteins of varying a-helical content are self-assembled with a common template, trypsin hydrolyzed gliadin (THGd). It is found that the amount of high strand density �-sheet formed is approximately equal to the amount of a-helix lost in the adder protein. However, the amount of a-helix converted is much less than the total a-helix content of the adder protein. Fourier transform-infrared (FTIR) spectroscopy analysis of the conformation change indicates hydrophobic interactions are important. A strong correlation is found between the conformation change and hydrophobic regions of the a-helix in the adder protein.

Influence of conformation change on the hierarchical self-assembly of amyloid fibers

247th National Meeting (2014)

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