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It is known that the process of amyloid fibril formation, including amyloid β (Aβ) and islet amyloid polypeptide, is generally associated with diseases, such as Alzheimer’s disease, type II diabetes, and prion diseases. However, many proteins form amyloid-like fibrils but do not associate with amyloidrelated diseases. Amyloid fibrils are elongated, insoluble structures of 7-10 nm in diameter found in extracellular plaques. Structural studies have shown that mature amyloid fibrils involve the alignment of short peptide segments, usually between 6 and 12 residues in length, from many protein monomers. Together, these aligned polypeptide stretches form the characteristic core structure of the amyloid fibril, the cross β sheet, in which β strands run perpendicular to the main axis of the fibril. Amyloid fibrils possess a characteristic UV absorbing spectrum at the peak of 540 nm with Congo red and a characteristic X-ray diffraction pattern. Thus, specific pattern of molecular interactions, rather than nonspecific hydrophobic interactions, lead to ordered structures. Nevertheless, common structural elements responsible for such organized structures have not been identified and the mechanism of amyloid fibril formation is unclear. Previously, we screened the synthetic peptide library derived from the laminin-111 sequence, and identified five amyloidgenic peptides, A119 (LSNIDYILIKAS, mouse laminin α1 chain, 1321-1332), A208 (AASIKVAVSADR, mouse laminin α1 chain, 2097-2108), AG97 (SAKVDAIGLEIV, mouse laminin α1 chain, 2942-2953), B133 (DISTKYFQMSLE, mouse laminin β1 chain, 1367-1378), and B160 (VILQQSAADIAR, mouse laminin β1 chain, 1607-1618) [1]. Laminins, major components of basement membranes, regulate multiple biological functions, including cell adhesion, migration, differentiation, neurite outgrowth, wound healing, angiogenesis, and tumor progression. Laminins are a family of heterotrimeric glycoproteins that consist of α, β, and γ chains. So far, five α, three β, and three γ chains have been identified and at least 16 laminin isoforms have been reported that are formed by various combinations of each chains. Here, we focused on the AG97 and B160 peptide, which exhibits amyloid-like fibril formation, heparin-dependent cell attachment activity, and neurite outgrowth activity. Our approach was to investigate the essential residues for fibril formation and cell behavior using alanine-substituted peptides.

Structural Requirement of Fibrogenic Peptide AG97 (SAKVDAIGLEIV) and B160 (VILQQSAADIAR) for Amyloid-Like Fibril Formation and Cellular Activity