Abstract
Introduction Serum amyloid A (SAA) is an acute phase protein associated with pathological amyloid deposits. The present study was aimed toward identification of the minimal amyloid-forming fragment of human SAA1 [1]. This information may lead to a better understanding of the pathological process of amyloidogenesis and direct to the design of amyloid inhibitors of clinical value. Employing synthetic peptides relevant to the known SAA amyloidogenic domain (i.e. SAA 1→12 RSFFSFLGEAFD) [2] we show that amyloid formation can be easily achieved with the pentapeptide SAA 2→6 (Figure 1, A). Moreover, we were able to identify a secondary amyloidogenic domain (SAA 50→59: GGAWAAEVIS) within the human SAA (Figure 1, C).
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