The conformation-sensitive amide I band in the Fourier transform infrared (FTIR) spectra of amyloid A suspensions in D2O was examined as a function of temperature (25-95 °C) and applied hydrostatic pressure (1-12 kbar) to assess the stability of the peptide. The principal changes observed upon heating were a significant loss of intermolecular β-sheet structure, and an increase in the broad band centred at 1644 cm-1 assigned to unordered structure and α-helices of the dissociated species. Application of hydrostatic pressure at ambient temperature resulted in a limited degree of aggregate dissociation. These structural changes were partially reversible with cooling or release of the applied pressure. Dissolving the aggregated peptide in alkaline solution (pH 12) also resulted in disaggregation. Dissociation of organ-deposited amyloid substance bears clinical relevance. The present data indicate that residual amounts of undissociated amyloid in the milieu at physiological and acidic pH may act as nucleating foci rendering dissociated amyloid to reaggregate into organized amyloid.