Determination of Regions Involved in Amyloid Fibril Formation for Ap(1-40) Peptide
The study of amyloid structures and the process of their formation is an important problem of biophysics. One of the aspects of such studies is to determine the amyloidogenic regions of protein chain that form the spine of an amyloid fibril. We have theoretically predicted the amyloidogenic regions of the AP(1-40) peptide capable of forming an amyloid structure. These regions are from 16 to 21 and from 32 to 36 amino acid residues. In this paper we have attempted to identify these sites experimentally by the method of tandem mass spectrometry. As a result, it was shown that regions of the AP(1-40) peptide from 16 to 22 and from 28 to 40 amino acid residues are resistant to proteases, i.e. are included in the spine of amyloid fibrils. Our results correlate with the results of the theoretical prediction.