From the globular to the fibrous state: protein structure and structural conversion in amyloid formation
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The term ‘amyloid’ was used originally to describe certain deposits found post-
mortem in organs and tissues, which gave a positive reaction when
stained with iodine (Virchow, 1854). Only later was it realized that the material was
in fact predominantly proteinaceous, although it is known to be associated with
carbohydrates, particularly glucosoaminoglycans, when obtained from many
ex vivo sources. With the increasing precision in the definition of amyloid,
initially from its characteristic green birefringence when stained with the dye Congo
Red (Missmahl & Hartwig, 1953), and later from its particular appearance
under the electron microscope (Cohen & Calkins, 1959) and its X-ray diffraction
pattern (Eanes & Glenner, 1968), it has become evident that it is a specific
fibrillar protein state, which can also be formed by some proteins when denatured in
vitro (Burke & Rougvie, 1972), and by synthetic oligopeptides (Bradbury et al .
1960) that may form amyloid spontaneously when placed in pure aqueous medium (Serpell,
1996). Although these latter may form useful experimental systems for the
study of amyloid, its major interest at present is that it is associated with
a number of prominent lethal diseases (Benson & Wallace, 1989; Pepys, 1994).