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Proteins have native functional states but can also form amyloid fibrils (Fowler et al .,2007, Maji et al., 2009, Dobson et al., 2003). In the amyloid state, proteins are denaturated and aggregated with -sheet-rich structures. Accumulation of amyloids can result in protein amyloidosis, which has attracted much attention. Amyloidosis is associated with many serious neurodegenerative diseases, such as Alzheimer’s disease (Sipe et al., 1992), dialysisrelated amyloidosis (Rochet et al., 2000), prion disease (Prusiner, 1998), and type II diabetes (Ahmad et al., 2004). Consequently, it is important to clarify the mechanism of amyloidosis, so that it can be inhibited or controlled. Amyloid structures have been analyzed by various methods including nuclear magnetic resonance (NMR) spectroscopy, electron microscopy, X-ray spectroscopy and Fourier transform infrared (FTIR) spectroscopy. Theoretical calculations of amyloidosis have also been conducted (Miller et al., 2010). Protein amyloidosis is affected by environmental conditions such as the temperature (Kusumoto et al., 1998), pH (Petkova et al., 2004), and ionic strength (Zidar et al., 2011), and by nucleation (Kanji et al., 2008). Because amyloidosis occurs at the cell surface, the interaction between the protein and cell interface is also important (Xu et al., 2005). Therefore, the amyloidosis of proteins can be controlled by manipulating the environmental conditions. However, it has been reported that artificial additives, such as metal ions (Chanki et al., 2007), peptides (Suzuki et al., 2010), sugars (Anubhav et al., 2004) and nanoparticles (Saraiva et al., 2010), can alter the environmental conditions and affect amyloidosis. Because amyloidosis occurs in vivo, the molecules on the cell surfaces are of interest as additives to control amyloidosis. It has been reported that protein amyloidosis with Amyloid beta (A) (Alzheimer’s disease) (McLaurin et al., 1996), 2-microglobulin (dialysisrelated amyloidosis) (Bourgault et al., 2011), and prion protein (Pan et al., 2002) formation is affected by interactions with glycosaminoglycans (GAGs) on the cell surfaces. This affects all these proteins, even though they have different amino acid sequences and native protein structures. GAGs are long unbranched polysaccharides of repeating disaccharide subunits of hexosamines (glucosamine and galactosamine) and uronic acid (glucuronic acid and iduronic acid) (Rudd et al., 2010). Well-known GAGs are heparin, chondroitin sulfate, keratin sulfate, dermatan sulfate and hyaluronic acid. Most GAGs are highly sulfonated. The interaction of proteins with GAGs is important in amyloidosis, but it is difficult to analyze the detail of this interaction because GAGs have complex structures and high molecular weights.

Interaction and Aggregation of Amyloid β Peptide with Multivalent Sulfonated Sugar