Single amino acids (phenylalanine, tyrosine and glycine) have been evaluated for fibrillar structure under neutral, aqueous conditions using scanning electron microscopy, transmission electron microscopy, circular dichroism, FTIR, and Congo red and thioflavin T histological dye assays. All these techniques prove that aromatic amino acids, such as phenylalanine and tyrosine, do in fact form distinct fibrillar structures albeit without any secondary structural characteristics such as an alpha-helix or a beta-sheet. The nature of the interactions between neighbouring amino acids in the fibrillar structures are purported to simply be non-covalent pi-pi interactions.
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