The molecular conformation of amyloid fibril revealed by pressure axis

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The pressure-induced changes in the secondary structure of insulin amyloid fibril up to 1100MPa were studied by means of the high pressure Fourier transform infrared spectroscopy. The early amyloid fibril to come from intermediate state of insulin was melted by high compression up to 550MPa. But the aged amyloid fibril does not change to be rigid structure by very high compression up to 1GPa.The detail structure of insulin under high pressure was studied by high pressure one- and two-dimensional NMR spectroscopy. High pressure NMR showed large changes in amide proton chemical shift for the residues mainly in the N- and C-terminal strands of B chain and helix1 of A-chain. The structural changes in the N- and C-terminal strands of B-chain under high pressure is a key factor for the pressure induced molecular association and aggregation of insulin