Amyloid fibril formation is believed to be a nucleation-dependent polymerization process which may be influenced by various other factors with important consequences for the development, prevention or treatment of
amyloidosis. We have previously shown that
laminin inhibits A beta
peptide fibril formation in vitro. Here we present a kinetic study that indicates
laminin to be a potent anti-
amyloidosis factor, as it not only inhibited
A beta 1-40 fibril aggregation, but also inhibited the aggregation of the Dutch
A beta 1-40 variant, a
peptide with a higher capacity to aggregate than the wild-type
A beta 1-40. The inhibitory effect of
laminin on
amyloid fibril formation was not overcome by the addition of pre-formed A beta fibrils, suggesting that
laminin inhibits the fibril elongation process. At the present time, however, we cannot rule out the possibility that
laminin also affects the initial nucleation process of A beta fibril formation. On other hand,
laminin was not able to counteract the
amyloid fibril formation promoted by
acetylcholinesterase (AChE), another component of the
amyloid deposits found in AD brains. The effect of
laminin may be important as an inhibitor of A beta amyloidogenesis in vivo, specifically at the level of cerebral blood vessels.